|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
44-364 |
4.17e-84 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 258.44 E-value: 4.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 44 WWFLTRN---EETTDDAFTDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLAVAQLHQA 120
Cdd:COG1566 23 LWAAGRNgpdEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 121 QAQLALskvqyPAQRDEAKAQVLKAQADMANAQAEY-RRQRGVDPRATTQQSIDAANAQLRSAQAGLASAQAQLEVAEQv 199
Cdd:COG1566 103 EAELGA-----EAEIAAAEAQLAAAQAQLDLAQRELeRYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQA- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 200 qlQIRQQETNVEArERQVDQARAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKES 278
Cdd:COG1566 177 --GLREEEELAAA-QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDdLWVEAYVPET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 279 QLERMKPGDKVTVSVDAWPDMALEGHIDSIQQGSGsrfSAFPSENATGNfvkIVQRVPVKIVIDKGLDpnKPLPLGLSVE 358
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAG---FTSPPKNATGN---VVQRYPVRIRLDNPDP--EPLRPGMSAT 325
|
....*.
gi 771285631 359 PKVTVE 364
Cdd:COG1566 326 VEIDTE 331
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
44-361 |
8.23e-76 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 237.38 E-value: 8.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 44 WWFLTRNE-ETTDDAFTDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLAVAQLHQAQA 122
Cdd:TIGR00998 22 YWFLVLRDyESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAELALAKAEANLAALVRQTKQLEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 123 QLAlskvQYPAQRDEAKAQVLKAQADMANAQAEYRR-----QRGVDPRATTQQSIDAanaqlrsaqagLASAQAQLEVAE 197
Cdd:TIGR00998 102 TVQ----QLQAKVESLKIKLEQAREKLLQAELDLRRrvplfKKGLISREELDHARKA-----------LLSAKAALNAAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 198 QVQLQIRQQETNVEA--RERQVDQARAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSP-NVWVVAN 274
Cdd:TIGR00998 167 QEQLNANQALVRGTPlkKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAeQMYVEAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 275 FKESQLERMKPGDKVTVSVDAWP-DMALEGHIDSIQQGSGSRFSAFPSENATGNFVKIVQRVPVKIVIDKGLDPNKPLPL 353
Cdd:TIGR00998 247 FKETQLKNVRIGQPVTIRSDLYGsDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRI 326
|
....*...
gi 771285631 354 GLSVEPKV 361
Cdd:TIGR00998 327 GLSAEVEI 334
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
44-361 |
1.70e-54 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 183.74 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 44 WWFLT-RNEETTDDAFTDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLAVAQLHQaqa 122
Cdd:PRK15136 41 YWFLVlRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQ--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 123 QLALSKvQYPAQRDEAKAQVLKAQADMAnaqaeyRRqrgvdprattqQSIDAANA----QLRSAQAGLASAQAQLEVAEQ 198
Cdd:PRK15136 118 LMINSK-QYQANIELQKTALAQAQSDLN------RR-----------VPLGNANLigreELQHARDAVASAQAQLDVAIQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 199 vQLQIRQQ---ETNVEaRERQVDQARAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLV-SPNVWVVAN 274
Cdd:PRK15136 180 -QYNANQAmilNTPLE-DQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVpATNLWVDAN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 275 FKESQLERMKPGDKVTVSVDAW-PDMALEGHIDSIQQGSGSRFSAFPSENATGNFVKIVQRVPVKIVIDKGLDPNKPLPL 353
Cdd:PRK15136 258 FKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRI 337
|
....*...
gi 771285631 354 GLSVEPKV 361
Cdd:PRK15136 338 GLSTLVTV 345
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
53-343 |
1.08e-49 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 170.21 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 53 TTDDAFTDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLavaqlhqAQAQLALSKVQYP 132
Cdd:PRK10476 38 STDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAL-------ADAQIMTTQRSVD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 133 AQR---DEAKAQVLKAQADMANAQAEYRRQRGVDPRA-TTQQSIDAANAQLRSAQAGLASAQAQLEVAEQVQlqirqqeT 208
Cdd:PRK10476 111 AERsnaASANEQVERARANAKLATRTLERLEPLLAKGyVSAQQVDQARTAQRDAEVSLNQALLQAQAAAAAV-------G 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 209 NVEARERQVDQARAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPNVW-VVANFKESQLERMKPGD 287
Cdd:PRK10476 184 GVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWyAIANFRETDLKNIRVGD 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 771285631 288 KVTVSVDAWPDMALEGHIDSIQQG-----SGSRFSAFPSENATGNFVKIVQRVPVKIVIDK 343
Cdd:PRK10476 264 CATVYSMIDRGRPFEGKVDSIGWGvlpddGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDK 324
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
62-364 |
1.45e-45 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 158.57 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 62 DVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLglavaqlhqaqaqlalskvqypaqrdeakaq 141
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQL------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 142 vLKAQADMANAQAEYRRQRG-VDPRATTQQSIDAANAQLRSAQAglasaqaqlevaeqvqlqirqqetnvearerQVDQA 220
Cdd:COG0845 71 -AAAQAQLELAKAELERYKAlLKKGAVSQQELDQAKAALDQAQA-------------------------------ALAAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 221 RAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAWPDM 299
Cdd:COG0845 119 QAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDpLEVEFDVPESDLARLKVGQPVTVTLDAGPGK 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 771285631 300 ALEGHIDSIQqgsgsrfsafPSENATgnfvkiVQRVPVKIVIDkglDPNKPLPLGLSVEPKVTVE 364
Cdd:COG0845 199 TFEGKVTFID----------PAVDPA------TRTVRVRAELP---NPDGLLRPGMFVRVRIVLG 244
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
47-315 |
1.95e-42 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 150.27 E-value: 1.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 47 LTRNEETTDDAFTDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLAVAQLHQAQA---- 122
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAeldr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 123 ---------QLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRRQRGVDPR-ATTQQSIDAANAQLRSAQAGLASAQAQ 192
Cdd:pfam00529 84 lqaleselaISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIgGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 193 L-----EVAEQVQLQIRQQETNVEARERQVDQARAQLETANLNLSYTEVRAPFDGFVTKRNVQP-GTLVQAGTALFSLVS 266
Cdd:pfam00529 164 LdqiyvQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 771285631 267 PN-VWVVANFKESQLERMKPGDKVTVSVDAWPD---MALEGHIDSIQQGSGSR 315
Cdd:pfam00529 244 EDnLLVPGMFVETQLDQVRVGQPVLIPFDAFPQtktGRFTGVVVGISPDTGPV 296
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
44-305 |
8.38e-35 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 130.08 E-value: 8.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 44 WWFLTRNeettDDAFT-DGDV----VTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDprDTTAQRDQAQAQLGLAVAQlh 118
Cdd:PRK03598 23 WWYQSRQ----DNGLTlYGNVdirtVNLGFRVGGRLASLAVDEGDAVKAGQVLGELD--AAPYENALMQAKANVSVAQ-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 119 qaqAQLALSKVQY-PAQRDEAKAQVLKAQADMANAQAEYRRQRGVDP-RATTQQSIDAANAQLRSAQAGLASAQAQLEva 196
Cdd:PRK03598 95 ---AQLDLMLAGYrDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKsRTISANDLENARSSRDQAQATLKSAQDKLS-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 197 eQVQLQIRQQEtnVEARERQVDQARAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALF--SLVSPnVWVVAN 274
Cdd:PRK03598 170 -QYREGNRPQD--IAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFtlSLTRP-VWVRAY 245
|
250 260 270
....*....|....*....|....*....|.
gi 771285631 275 FKESQLERMKPGDKVTVSVDAWPDMALEGHI 305
Cdd:PRK03598 246 VDERNLGQAQPGRKVLLYTDGRPDKPYHGQI 276
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
61-308 |
1.03e-32 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 124.35 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 61 GDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDttaqrdqAQAQLGLAVAQLHQAQAQLALSKVQYPaqrdeaka 140
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDD-------YQLALQAALAQLAAAEAQLELAQRSFE-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 141 qvlkaqadmanaqaeyRRQRGVDPRATTQQSIDAANAQLRSAQAglasaqaqlevaeqvqlqirqqetnvearerQVDQA 220
Cdd:TIGR01730 89 ----------------RAERLVKRNAVSQADLDDAKAAVEAAQA-------------------------------DLEAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 221 RAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAWPDM 299
Cdd:TIGR01730 122 KASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDpLEADFSVPERDLPQLRRGQTLTVELDALPGE 201
|
....*....
gi 771285631 300 ALEGHIDSI 308
Cdd:TIGR01730 202 EFKGKLRFI 210
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
44-354 |
6.72e-30 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 116.38 E-value: 6.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 44 WWFLTRNEETTDDAFTdGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDprdttaqrdqaqaqlglavaqlhQAQAQ 123
Cdd:PRK10559 29 WVFYTESPWTRDARFS-ADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTID-----------------------QPRYQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 124 LALskvqypaqrDEAKAQVLKAQADMANAQAEYRRQRGVDPRATTQQSIDAANAQLRSAQAGLASAQAQLEVAEqvqlqi 203
Cdd:PRK10559 85 KAL---------AEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAK------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 204 rqqetnvearerqvdqaraqletanLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLER 282
Cdd:PRK10559 150 -------------------------LDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNsFYVLAYMEETKLEG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 283 MKPGDKVTVSvdawP---DMALEGHIDSIQQG----SGSRFS-AFPSENATGNFVKIVQRVPVKIVIDKglDPNKPLPLG 354
Cdd:PRK10559 205 VRPGYRAEIT----PlgsNKVLKGTVDSVAAGvtnsSSTRDSkGMATIDSNLEWVRLAQRVPVRIRLDN--QQGNLYPAG 278
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
62-308 |
1.01e-19 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 86.41 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 62 DVVTIAPKTAGYVTELRVRDN-QRVKKGDVLVVID-Prdttaqrdqaqaqlglavaqlhqaqaqlalskvqypaqrdeak 139
Cdd:pfam16576 18 RLAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYsP------------------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 140 aqvlkaqaDMANAQAEYRRQRGVDPRATTQQSIDAANAQLRsaqaglasaqaQLEVAEQvqlQIRQQEtnveaRERQVDQ 219
Cdd:pfam16576 55 --------ELVAAQQEYLLALRSGDALSKSELLRAARQRLR-----------LLGMPEA---QIAELE-----RTGKVQP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 220 araqletanlnlsYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVS-PNVWVVANFKESQLERMKPGDKVTVSVDAWPD 298
Cdd:pfam16576 108 -------------TVTVYAPISGVVTELNVREGMYVQPGDTLFTIADlSTVWVEADVPEQDLALVKVGQPAEVTLPALPG 174
|
250
....*....|
gi 771285631 299 MALEGHIDSI 308
Cdd:pfam16576 175 KTFEGKVDYI 184
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
59-364 |
1.37e-13 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 71.58 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 59 TDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLAVAQLHQAQA---------------- 122
Cdd:TIGR01843 39 PSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAeadsqaaiefpddlls 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 123 --------QLALSKVQYPAQRDE-----------------------AKAQVLKAQADMANAQAEYRRQ---RGVDPRATT 168
Cdd:TIGR01843 119 aedpavpeLIKGQQSLFESRKSTlraqlelilaqikqleaelaglqAQLQALRQQLEVISEELEARRKlkeKGLVSRLEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 169 ---QQSIDAANAQLRSAQAGLASAQAQLevaEQVQLQIRQ-QETNVEARERQVDQARAQLETANLNLS-------YTEVR 237
Cdd:TIGR01843 199 lelERERAEAQGELGRLEAELEVLKRQI---DELQLERQQiEQTFREEVLEELTEAQARLAELRERLNkardrlqRLIIR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 238 APFDGFV-TKRNVQPGTLVQAGTALFSLVSPNV--WVVANFKESQLERMKPGDKVTVSVDAWPDM---ALEGHIDSIQQg 311
Cdd:TIGR01843 276 SPVDGTVqSLKVHTVGGVVQPGETLMEIVPEDDplEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRrygILNGKVKSISP- 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 771285631 312 sgsrfSAFPSENATGNFVKIVQRVPVKIVIDKgldpnkplPLGLSVEPKVTVE 364
Cdd:TIGR01843 355 -----DTFTDERGGGPYYRVRISIDQNTLGIG--------PKGLELSPGMPVT 394
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
64-309 |
1.48e-13 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 70.96 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 64 VTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGLAVAQLHQAQAQLALSKVQYPAQRDEAKAQvl 143
Cdd:PRK11578 62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQ-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 144 kaqadmanaqaeyrrqrgvdprATTQQSIDAANAQLRSAQAGLASAQAqlevaeqvqlqirqqetnvearerQVDQARAQ 223
Cdd:PRK11578 140 ----------------------AVSQQDLDTAATELAVKQAQIGTIDA------------------------QIKRNQAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 224 LETANLNLSYTEVRAPFDGFVTKRNVQPGTLV----QAGTALFSLVSPNVWVVANFKESQLERMKPGDKVTVSVDAWPDM 299
Cdd:PRK11578 174 LDTAKTNLDYTRIVAPMAGEVTQITTLQGQTViaaqQAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLT 253
|
250
....*....|
gi 771285631 300 ALEGHIDSIQ 309
Cdd:PRK11578 254 RYEGVLKDIL 263
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
235-322 |
5.15e-13 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 64.69 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 235 EVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAWPDMALEGHIDSIQQGSG 313
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDrLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
....*....
gi 771285631 314 SRFSAFPSE 322
Cdd:pfam13437 81 PDTGVIPVR 89
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
62-110 |
2.31e-11 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 58.22 E-value: 2.31e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 771285631 62 DVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQL 110
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQL 49
|
|
| 8a0102 |
TIGR00999 |
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ... |
83-293 |
1.95e-10 |
|
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]
Pssm-ID: 273386 [Multi-domain] Cd Length: 265 Bit Score: 60.53 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 83 QRVKKGDVLVVIDPRDTTAQRDQaqaqlglavaqLHQAQAQLALSKVQYpaqrdEAKAQVLkaqadmanaqaeyrrQRGV 162
Cdd:TIGR00999 2 DPVKKGQVLAVVDSPELAKMAAE-----------LKVAQKRVELARKTY-----EREKKLF---------------EQGV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 163 dpraTTQQSIDAANAQLRSAQAGLASAQAQLEVAEQVQlqirqqetnvearerqvdqaraqletanlNLSYTEVRAPFDG 242
Cdd:TIGR00999 51 ----IPRQEFESAEYALEEAQAEVQAAKSELRSAREAK-----------------------------DGSYVEVRSPFDG 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 771285631 243 FVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSV 293
Cdd:TIGR00999 98 YITQKSVTLGDYVAPQAELFRVADLGaVWVEAEVPAKDVSRIRKGSKATVLL 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-225 |
1.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 102 QRDQAQAQLGLAVAQLHQAQAQLALSKvqypAQRDEAKAQVLKAQADMANAQAEYRRQRgvdprattqQSIDAANAQLRS 181
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELR---------LELEELELELEE 285
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 771285631 182 AQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLE 225
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
162-260 |
1.16e-07 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 53.18 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 162 VDPrATTQQSIDAANAQLRSAQAglASAQAQLEVAEQVQL----QIRQQETNVEARERQ-----VDQARAQLETANLNLS 232
Cdd:PRK15030 96 IDP-ATYQATYDSAKGDLAKAQA--AANIAQLTVNRYQKLlgtqYISKQEYDQALADAQqanaaVTAAKAAVETARINLA 172
|
90 100
....*....|....*....|....*...
gi 771285631 233 YTEVRAPFDGFVTKRNVQPGTLVQAGTA 260
Cdd:PRK15030 173 YTKVTSPISGRIGKSNVTEGALVQNGQA 200
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
59-260 |
3.18e-07 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 51.71 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 59 TDGDVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPRdttaqrdqaQAQLGLAvaqlhQAQAQLAlskvqypaqrdea 138
Cdd:PRK11556 83 TAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPR---------PFKVALA-----QAQGQLA------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 139 kaqvlKAQADMANAqaeyRRqrgvdprattqqsiDAANAQlRSAQAGLASAQaqlEVAEQVQLqIRQQETNVEARERQVD 218
Cdd:PRK11556 136 -----KDQATLANA----RR--------------DLARYQ-QLAKTNLVSRQ---ELDAQQAL-VSETEGTIKADEASVA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 771285631 219 QARaqletanLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTA 260
Cdd:PRK11556 188 SAQ-------LQLDYSRITAPISGRVGLKQVDVGNQISSGDT 222
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
69-255 |
3.82e-07 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 51.33 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 69 KTAGYVTELRVRDNQRVKKGDVLVVIDPRDTTAQRDQAQAQLGlavaqlhqaqaqlalskvqypaqrdeakaqvlKAQAD 148
Cdd:PRK09578 69 RVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALA--------------------------------KAEAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 149 MANAQAEYRRQRG-VDPRATTQQSIDAANAQLRSAQAGLASaqaqlevaeqvqlqirqqetnvearerqvdqARAQLETA 227
Cdd:PRK09578 117 HLAALDKRRRYDDlVRDRAVSERDYTEAVADERQAKAAVAS-------------------------------AKAELARA 165
|
170 180
....*....|....*....|....*...
gi 771285631 228 NLNLSYTEVRAPFDGFVTKRNVQPGTLV 255
Cdd:PRK09578 166 QLQLDYATVTAPIDGRARRALVTEGALV 193
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-227 |
4.87e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 97 RDTTAQRDQAQAQLGLAVAQLHQAQAQLALSKvqypAQRDEAKAQVLKAQADMANAQAEYRR--------QRGVDP---- 164
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELE----AELEELRLELEELELELEEAQAEEYEllaelarlEQDIARleer 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 771285631 165 RATTQQSIDAANAQLRSAQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLETA 227
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
98-226 |
1.23e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 98 DTTAQRDQAQAQLGLAVAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQ-AEYRRQRGVD-PRA-TTQQSIDA 174
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAElAELSARYTPNhPDViALRAQIAA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 771285631 175 ANAQLRS-AQAGLASAQAQLEVAEQVQLQIRQQETNVEAR--------------ERQVDQARAQLET 226
Cdd:COG3206 303 LRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARlaelpeleaelrrlEREVEVARELYES 369
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
100-225 |
1.84e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 100 TAQRDQAQAQLgLAVAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRRQRgvdprattqqsiDAANAQl 179
Cdd:COG2268 198 IRDARIAEAEA-ERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREA------------ETARAE- 263
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 771285631 180 RSAQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLE 225
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEAD 309
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
105-232 |
1.78e-05 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 46.18 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 105 QAQAQLGLAVAQLHQAQAQLALSKV-----QYPAQRDEAKAQVLKAQADMANAQAEYRRQ--RGVDPRATTQQSIDAANA 177
Cdd:COG1538 18 AARARVEAARAQLRQARAGLLPSQEldlggKRRARIEAAKAQAEAAEADLRAARLDLAAEvaQAYFDLLAAQEQLALAEE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 771285631 178 QLRSAQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLETANLNLS 232
Cdd:COG1538 98 NLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNALA 152
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
62-260 |
1.86e-05 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 46.25 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 62 DVVTIAPKTAGYVTELRVRDNQRVKKGDVLVVIDPrdttaqrdqaqaqlglavaqlhqAQAQLALskvqypaqrDEAKAQ 141
Cdd:PRK09859 60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDP-----------------------APLQAEL---------NSAKGS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 142 VLKAQADMANAQAEYRRQRGV-DPRATTQQSIDAANAQLRSAQAglasaqaqlevaeqvqlqirqqetnvearerQVDQA 220
Cdd:PRK09859 108 LAKALSTASNARITFNRQASLlKTNYVSRQDYDTARTQLNEAEA-------------------------------NVTVA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 771285631 221 RAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTA 260
Cdd:PRK09859 157 KAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQA 196
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
91-233 |
2.94e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 91 LVVIDPRDTTAQR-DQAQAQLGLAVAQLHQAQAQLAlskvQYPAQRDEAKAQVLkaqADMANAQAEYRRQRGVDPRATTQ 169
Cdd:PRK11281 69 LALLDKIDRQKEEtEQLKQQLAQAPAKLRQAQAELE----ALKDDNDEETRETL---STLSLRQLESRLAQTLDQLQNAQ 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 771285631 170 QSIDAANAQLRSAQAGLASAQAQLEVAEQVQLQIRQQETNVEA-----RERQVDQARAQLETANLNLSY 233
Cdd:PRK11281 142 NDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVggkalRPSQRVLLQAEQALLNAQNDL 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
112-238 |
4.87e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 112 LAVAQLHQAQAQLALSKVQYpAQRDEAKAQVLKAQADMANAQAEYRRQRGVDPRATTQQSIDAANAQLRSAQAGLASAQA 191
Cdd:COG4717 68 LNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 771285631 192 QLEVAEQVQLQIRQQETNVEARERQVDQARAQLETANLNLSYTEVRA 238
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-227 |
5.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 85 VKKGDVLVVIDPRDTTAQR----DQAQAQLGLAVAQLHQAQAQLALSKvqypAQRDEAKAQV--LKAQADMANAQAEYRR 158
Cdd:COG4913 583 VKGNGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAE----ERLEALEAELdaLQERREALQRLAEYSW 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 159 QRgVDpRATTQQSIDAANAQLRSAQAG---LASAQAQLEVAEQ-----------VQLQIRQQETNVEARERQVDQARAQL 224
Cdd:COG4913 659 DE-ID-VASAEREIAELEAELERLDASsddLAALEEQLEELEAeleeleeeldeLKGEIGRLEKELEQAEEELDELQDRL 736
|
...
gi 771285631 225 ETA 227
Cdd:COG4913 737 EAA 739
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
102-234 |
5.09e-05 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 45.06 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 102 QRDQAQAQLGLAVAQLHQAQAQLALSK-------------VQYPAQRDEAKAQVLKAQADMANAQAEYRRQRGV-DPRAT 167
Cdd:TIGR01844 121 EVLRAQEILALAEANLAALKEQLDLARarfdvglgtrtdvLQAEARYASARAQLIQAQNNLDDAKAQLRRLVGQpELAPL 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 771285631 168 TQQSIDAANAQlrsaqaglaSAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQ-LETANLNLSYT 234
Cdd:TIGR01844 201 AVPSFPAELPE---------PLDQLLEIAEASNPLLLAAQAAVDAARYQVEQARAGhLPTLSLTASTG 259
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
137-231 |
5.25e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.72 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 137 EAKAQVLKAQADMANAQAEYRRQrgvdprattQQSIDAANAQLRSAQAGLASAQAQleVAEQVQLQIRQQETNVEARERQ 216
Cdd:TIGR04320 265 TAQADLAAAQTALNTAQAALTSA---------QTAYAAAQAALATAQKELANAQAQ--ALQTAQNNLATAQAALANAEAR 333
|
90
....*....|....*
gi 771285631 217 VDQARAQLETANLNL 231
Cdd:TIGR04320 334 LAKAKEALANLNADL 348
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
105-224 |
1.05e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 43.87 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 105 QAQAQLGLAVAQLHQAQAQLALSKVQYPA-------------QRDEAKAQVLKAQADMANAQAEYRRQRGVDPRATTQqs 171
Cdd:COG1538 87 AAQEQLALAEENLALAEELLELARARYEAglasrldvlqaeaQLAQARAQLAQAEAQLAQARNALALLLGLPPPAPLD-- 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 771285631 172 idaANAQLRSAQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQL 224
Cdd:COG1538 165 ---LPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEIGVARAAF 214
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
97-225 |
1.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 97 RDTTAQRDQAQAQLGLAVAQLhqAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRRQrgvDPRA-TTQQSIDAA 175
Cdd:COG3206 229 AEARAELAEAEARLAALRAQL--GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPN---HPDViALRAQIAAL 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 771285631 176 NAQLRS-AQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLE 225
Cdd:COG3206 304 RAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-235 |
2.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 97 RDTTAQRDQAQ--AQLGLAVAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRRQRgvdpRATTQQSIDA 174
Cdd:COG4913 245 EDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE----LERLEARLDA 320
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 771285631 175 ANAQLRSAQAGLASAQAQLEvaEQVQLQIRQQETNVEARERQVDQARAQLETANLNLSYTE 235
Cdd:COG4913 321 LREELDELEAQIRGNGGDRL--EQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
119-225 |
2.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 119 QAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEyrrqrgvdpraTTQQSIDAANAQLRSAQAGLASAQAQLEVAEQ 198
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELE-----------ELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100
....*....|....*....|....*..
gi 771285631 199 VQLQIRQQETNVEARERQVDQARAQLE 225
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLE 301
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
99-194 |
2.83e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.41 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 99 TTAQRDQAQAQLGLAVAQ--LHQAQAQLALSKVQyPAQrdEAKAQVLKAQADMANAQAEYrrqrgvdprattqqsiDAAN 176
Cdd:TIGR04320 278 NTAQAALTSAQTAYAAAQaaLATAQKELANAQAQ-ALQ--TAQNNLATAQAALANAEARL----------------AKAK 338
|
90
....*....|....*...
gi 771285631 177 AQLRSAQAGLASAQAQLE 194
Cdd:TIGR04320 339 EALANLNADLAKKQAALD 356
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
105-231 |
3.13e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 105 QAQAQLGLAVAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRrqrgvdpraTTQQSIDAANAQLRSAQA 184
Cdd:COG1538 241 SVGLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALR---------AAREQLEALEEALEAAEE 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 771285631 185 GLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLETANLNL 231
Cdd:COG1538 312 ALELARARYRAGLASLLDVLDAQRELLQAQLNLIQARYDYLLALVQL 358
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-237 |
4.16e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 101 AQRDQAQAQLGLAVAQLHQAQAQLALSKVQypAQRDEAKAQVLKAQADMANAQAEYRRQRgvdpRATTQQSIDAANAQLR 180
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEE--AANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIE 862
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 771285631 181 SAQAGLASAQAQLEVA------------------EQVQLQIRQQETNVEARERQVDQARAQLETANLNLSYTEVR 237
Cdd:TIGR02168 863 ELEELIEELESELEALlnerasleealallrselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
93-228 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 93 VIDPRDTTAQRDQAQAQlglaVAQLHQAQAQLALSKvqypAQRdEAKAQVLKAQADMANAQAEYRRQRGVDPRATT---Q 169
Cdd:COG4913 217 MLEEPDTFEAADALVEH----FDDLERAHEALEDAR----EQI-ELLEPIRELAERYAAARERLAELEYLRAALRLwfaQ 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 771285631 170 QSIDAANAQLRSAQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQ-----VDQARAQLETAN 228
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrLEQLEREIERLE 351
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-229 |
2.19e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 100 TAQRDQAQAQLGLAVAQLHQAQAQLALSKVQypAQRDEAKAQVLKAQADMANAQAEYRRQRgvdpRATTQQSIDAANAQL 179
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEER--RRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEEL 353
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 771285631 180 RSAQAGLASAQAQLE---------VAEQVQLQIRQQETNVEARERQVDQARAQLETANL 229
Cdd:COG1196 354 EEAEAELAEAEEALLeaeaelaeaEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
98-227 |
2.38e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 98 DTTAQRDQAQAQLG--LAVAQLHQAQAQLALSKvqypAQRDEAKA---QVLKAQADMANAQAEYRRQRGVdpRATTQQSI 172
Cdd:COG1842 48 QVIANQKRLERQLEelEAEAEKWEEKARLALEK----GREDLAREaleRKAELEAQAEALEAQLAQLEEQ--VEKLKEAL 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 771285631 173 DAANAQLRSAQAGLASAQAQLEVAEqVQLQIRQQETNVEAR---------ERQVDQARAQLETA 227
Cdd:COG1842 122 RQLESKLEELKAKKDTLKARAKAAK-AQEKVNEALSGIDSDdatsalermEEKIEEMEARAEAA 184
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
97-224 |
3.03e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 97 RDTTAQRDQAQAQLGLAVAQLHQAqaqLALSKvqypAQRDEAKAQVLKAQADMANAQAEyrrqrgvdpRATTQQSIDAAN 176
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADL---LSLER----QGNQDLQDSVANLRASLSAAEAE---------RSRLQALLAELA 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 771285631 177 AQLRSAQAGLASAQAQLEVAEQVQLQIRQQetnVEARERQVDQARAQL 224
Cdd:PRK09039 109 GAGAAAEGRAGELAQELDSEKQVSARALAQ---VELLNQQIAALRRQL 153
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-227 |
3.06e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 98 DTTAQRDQAQAQLGLAVAQLHQAQ-AQLALSKVQYPAQRDEAKAQVLKAQ-ADMANAQAEYRRQRGVDPRATTQ------ 169
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKReAQEEQLKKQQLLKQLRARIEELRAQeAVLEETQERINRARKAAPLAAHIkavtqi 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 771285631 170 -QSIDAANAQLRSAQAGLASAQAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLETA 227
Cdd:TIGR00618 306 eQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA 364
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
100-193 |
3.93e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.94 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 100 TAQRDQAQAQLGLAVAQLHQAQAQLALSKVQypAQRDEAKAQVLK-AQADMANAQAEYrrqrgvdprattqqsiDAANAQ 178
Cdd:TIGR04320 272 AAQTALNTAQAALTSAQTAYAAAQAALATAQ--KELANAQAQALQtAQNNLATAQAAL----------------ANAEAR 333
|
90
....*....|....*
gi 771285631 179 LRSAQAGLASAQAQL 193
Cdd:TIGR04320 334 LAKAKEALANLNADL 348
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
101-227 |
4.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 101 AQRDQAQ------AQLGLAVAQLHQAQAQLAlskvQYPAQRDEAKAQVLKAQADMANAQAEYRRQRGVDPRATTQQSIDA 174
Cdd:PRK04863 901 EQLDEAEeakrfvQQHGNALAQLEPIVSVLQ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDA 976
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 771285631 175 AnaQLRSAQAGLASA-QAQLEVAEQVQLQIRQQETNVEARERQVDQARAQLETA 227
Cdd:PRK04863 977 A--EMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS 1028
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
97-275 |
4.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 97 RDTTAQRDQAQAQLglavaqlhqAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRR-QRGVDPRATTQQSIDAA 175
Cdd:COG4717 98 EELEEELEELEAEL---------EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEElEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 176 NAQLRSAQAGLASAQAQLEVAEQVQLQ-----IRQQETNVEARERQVDQARAQLETANLNLSYTEVRApFDGFVTKRNVQ 250
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQdlaeeLEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKE 247
|
170 180
....*....|....*....|....*
gi 771285631 251 PGTLVQAGTALFSLVSPNVWVVANF 275
Cdd:COG4717 248 ARLLLLIAAALLALLGLGGSLLSLI 272
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-240 |
4.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 101 AQRDQAQAQLGLAVAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRRQRgvDPRATTQQSIDAANAQLR 180
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE--EALAEAEAALRDLRRELR 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 181 SAQAGLASaqaqlevaeqvqlqIRQQETNVEARerqVDQARAQLETAnlnLSYTEVRAPF 240
Cdd:COG4913 423 ELEAEIAS--------------LERRKSNIPAR---LLALRDALAEA---LGLDEAELPF 462
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
97-206 |
5.77e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.78 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 97 RDTTAQRDQAQAQLGLAVAQLHQAQAQLALSKVQ------------------YPAQRDEAKAQVLKAQADMANAQAEYRR 158
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQlqllnkllpqanlladetLADRLEELREELDAAQEAQAFIQQHGKA 918
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 771285631 159 QRGVDPRATTQQSIDAANAQLrsaqaglasaQAQLEVAEQVQLQIRQQ 206
Cdd:COG3096 919 LAQLEPLVAVLQSDPEQFEQL----------QADYLQAKEQQRRLKQQ 956
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-235 |
5.91e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.88 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 92 VVIDPRDTTAQRDQAQAQLGLAVAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQAdMANAQAEYRRQrgvdprattqqs 171
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE-LESRLEELEEQ------------ 380
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 771285631 172 IDAANAQLRSAQAGLASAQAQLEVAEQV--QLQIRQQETNVEARERQVDQARAQLETANLNLSYTE 235
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-226 |
6.03e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.21 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 124 LALSKVQYPAQRDEAKAQVLKAQADMANAQAEyrrqrgvdpRATTQQSIDAANAQLRSAQAGLASAQAQLEVAEQvqlQI 203
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKE---------LAALKKEEKALLKQLAALERRIAALARRIRALEQ---EL 78
|
90 100
....*....|....*....|...
gi 771285631 204 RQQETNVEARERQVDQARAQLET 226
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEA 101
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
133-237 |
7.66e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 38.10 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 133 AQRDEAKAQVLKAQADM-----ANAQAEYRRQRGVDPRATTQQSI-----------DAANAQLRSAQAGLASAQAQLEVA 196
Cdd:COG1538 198 AQLEAAEAEIGVARAAFlpslsLSASYGYSSSDDLFSGGSDTWSVglslslplfdgGRNRARVRAAKAQLEQAEAQYEQT 277
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 771285631 197 E-QVQLQIRQQETNVEARERQVDQARAQLETANLNLSYTEVR 237
Cdd:COG1538 278 VlQALQEVEDALAALRAAREQLEALEEALEAAEEALELARAR 319
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
115-227 |
8.28e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 37.12 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 115 AQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADMANAQAEYRrqrgvdpraTTQQSIDAANAQLRSAQAGLASAQAQLE 194
Cdd:pfam02321 76 ARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLE---------LAEQALELAEEALELAEARYEAGLISLL 146
|
90 100 110
....*....|....*....|....*....|...
gi 771285631 195 VAEQVQLQIRQQETNVEARERQVDQARAQLETA 227
Cdd:pfam02321 147 DVLQAEVELLEARLELLNAEADLELALAQLEQL 179
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
162-231 |
8.41e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 37.11 E-value: 8.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 771285631 162 VDPRATTQQSIDAANAQLRSAQAGLASAQAQlevAEQVQLQIRQQETNVEARERqvdQARAQLETANLNL 231
Cdd:COG1842 22 EDPEKMLDQAIRDMEEDLVEARQALAQVIAN---QKRLERQLEELEAEAEKWEE---KARLALEKGREDL 85
|
|
| |
