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Conserved domains on  [gi|446803550|ref|WP_000880806|]
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MULTISPECIES: GspE/PulE family protein [Enterobacteriaceae]

Protein Classification

GspE/PulE family protein( domain architecture ID 11457962)

GspE/PulE family protein similar to type II secretion system protein E, an essential component of type II systems, and to type IV pilus assembly ATPase PilB

CATH:  3.40.50.300
PubMed:  11226268
SCOP:  4005829|4004682

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
93-441 7.83e-64

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 216.98  E-value: 7.83e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  93 ISHAATLSASDLHITPGRDSTDFTYleaRVHGELELLDIVRKDEGLELLGATY--SGMtDVikgtqFDPGVPQDARLAer 170
Cdd:COG2804  187 LEDAIKEGASDIHIEPYEKRLRVRF---RIDGVLREVLRLPKSLAPALVSRIKimANL-DI-----AERRLPQDGRIK-- 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 171 fLKLAGL---FgaRYSHYPCVGGLYAVLRLIkDDSQHIPTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTGSGKSTTLR 247
Cdd:COG2804  256 -LRLGGReidL--RVSTLPTVYGEKVVLRIL-DKSAALLDLEQLGFSPDQLERLRRLIRRPHGIILVTGPTGSGKTTTLY 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 248 TAsaayLEQygFNDtggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAQGwvdsVKSALRLDPDAILNGEIRDHA 322
Cdd:COG2804  332 AA----LNE--LNT------PERNIITVEDPVEYQLPGINQVQVnpkigLTFASA----LRSILRQDPDVIMVGEIRDLE 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 323 SAITAIKAAMTGHLMLTTLHANDPINILERL-EMeGVQARMIADPqLfIGLLSQRLVQVICPHCRLPwHEVessrTDEER 401
Cdd:COG2804  396 TAEIAVQAALTGHLVLSTLHTNDAPSAITRLlDM-GVEPFLLASS-L-LGVLAQRLVRRLCPHCKEP-YEP----DPEEL 467
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446803550 402 RLVE-NFCQPDAVYLRNHNGCPHC-WRGVNGRTVIAEVISPD 441
Cdd:COG2804  468 ERLGlPPEELAPLTFYRGVGCEHCnGTGYKGRTGIYELLVID 509
 
Name Accession Description Interval E-value
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
93-441 7.83e-64

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 216.98  E-value: 7.83e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  93 ISHAATLSASDLHITPGRDSTDFTYleaRVHGELELLDIVRKDEGLELLGATY--SGMtDVikgtqFDPGVPQDARLAer 170
Cdd:COG2804  187 LEDAIKEGASDIHIEPYEKRLRVRF---RIDGVLREVLRLPKSLAPALVSRIKimANL-DI-----AERRLPQDGRIK-- 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 171 fLKLAGL---FgaRYSHYPCVGGLYAVLRLIkDDSQHIPTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTGSGKSTTLR 247
Cdd:COG2804  256 -LRLGGReidL--RVSTLPTVYGEKVVLRIL-DKSAALLDLEQLGFSPDQLERLRRLIRRPHGIILVTGPTGSGKTTTLY 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 248 TAsaayLEQygFNDtggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAQGwvdsVKSALRLDPDAILNGEIRDHA 322
Cdd:COG2804  332 AA----LNE--LNT------PERNIITVEDPVEYQLPGINQVQVnpkigLTFASA----LRSILRQDPDVIMVGEIRDLE 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 323 SAITAIKAAMTGHLMLTTLHANDPINILERL-EMeGVQARMIADPqLfIGLLSQRLVQVICPHCRLPwHEVessrTDEER 401
Cdd:COG2804  396 TAEIAVQAALTGHLVLSTLHTNDAPSAITRLlDM-GVEPFLLASS-L-LGVLAQRLVRRLCPHCKEP-YEP----DPEEL 467
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446803550 402 RLVE-NFCQPDAVYLRNHNGCPHC-WRGVNGRTVIAEVISPD 441
Cdd:COG2804  468 ERLGlPPEELAPLTFYRGVGCEHCnGTGYKGRTGIYELLVID 509
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
222-378 3.70e-54

PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.


Pssm-ID: 410873 [Multi-domain]  Cd Length: 159  Bit Score: 179.22  E-value: 3.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 222 RRMLQRPEGIVILSGPTGSGKSTTLRtASAAYLEQygfndtggillPRRRLFTIESPPEGRIPGAIQTAVMDTAQ-GWVD 300
Cdd:cd01129    4 RRLIKRPHGLILVTGPTGSGKTTTLY-AMLRELNG-----------PERNIITIEDPVEYQIPGINQSQVNEKIGlTFAD 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446803550 301 SVKSALRLDPDAILNGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADPqlFIGLLSQRLV 378
Cdd:cd01129   72 ALRAILRQDPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASA--LRGVIAQRLV 147
type_II_gspE TIGR02533
type II secretion system protein E; This family describes GspE, the E protein of the type II ...
84-436 5.63e-51

type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 131585 [Multi-domain]  Cd Length: 486  Bit Score: 180.65  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550   84 PVQQKMLGYISHAATLSASDLHITPGRDSTDFTYleaRVHGELEllDIVRKDEGLEllgatySGMTDVIK-GTQFDPG-- 160
Cdd:TIGR02533 107 PVIRLVNSLLSRAVKERASDIHIEPFEKALVVRF---RVDGVLR--DVLSPPKKLH------AALVSRVKiMAKLNIAek 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  161 -VPQDARLAerfLKLAGL-FGARYSHYPCVGGLYAVLRLIKDDSQHIpTFSMLGYHPEQERAVRRMLQRPEGIVILSGPT 238
Cdd:TIGR02533 176 rLPQDGRIS---LRVGGRdIDIRVSTVPTSHGERVVMRLLDKTAVRL-DLETLGMSPELLSRFERLIRRPHGIILVTGPT 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  239 GSGKSTTLRTAsAAYLEQygfndtggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAQGwvdsVKSALRLDPDAI 313
Cdd:TIGR02533 252 GSGKTTTLYAA-LSRLNT-----------PERNILTVEDPVEYQIEGIGQIQVnpkigLTFAAG----LRAILRQDPDII 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  314 LNGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADPQLfiGLLSQRLVQVICPHCRLPWHEve 393
Cdd:TIGR02533 316 MVGEIRDLETAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLL--GVLAQRLVRRLCPHCKEPYEA-- 391
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 446803550  394 ssrTDEERRLVeNFCQPDAVYLRNHNGCPHCWR-GVNGRTVIAE 436
Cdd:TIGR02533 392 ---TPEEIALF-GISPEGPINLYRPVGCPHCNHtGYLGRTGIYE 431
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
93-380 5.65e-48

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 166.69  E-value: 5.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550   93 ISHAATLSASDLHI-TPGRDstdfTYLEARVHGEL-ELLDIvrKDEGLELLGATYSGMTdviKGTQFDPGVPQDARLAER 170
Cdd:pfam00437   4 PLEALDEGASDIHVePPERI----VWIRFRVDGVLrEIPFP--DADALARLISRIKVMA---RLDISERRPPQDGRLPLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  171 FLKLAGLFgaRYSHYPCVGGLYAVLRLIKDDSQHIpTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTGSGKSTTLRTAS 250
Cdd:pfam00437  75 IGGKGVRV--RVSTLPTAGGEKLVIRLLDPSNVAL-SLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  251 aayleqyGFNDTggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAqgwvDSVKSALRLDPDAILNGEIRDHASAI 325
Cdd:pfam00437 152 -------GELNT-----RDENIVTVEDPVEIQLEGINQVQLnaragVTFA----DLLRAILRQDPDRIMVGEIRDLETAE 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446803550  326 TAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADPQLFIglLSQRLVQV 380
Cdd:pfam00437 216 IALQAANTGHLVLSTLHTNSAAGALTRLQDMGVPPFELASSLLLV--IAQRLVRK 268
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
93-379 7.81e-41

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 147.59  E-value: 7.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  93 ISHAATLSASDLHITPGRDSTDftyLEARVHGELELLDIVRKDEGLELLgaTY----SGMtdvikgtqfDPG---VPQ-- 163
Cdd:NF041000   4 IEEAIELRASDIHFLPREDGYQ---IKFRIGGGLIPYRELSLEEGQRLI--SYfkflAGM---------DIGekrRPQsg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 164 --DARLAER--FLKLA--GLFGARYShypcvgglyAVLRLIKDDSQHIPTFsmlgYHPEQERAVRRMLQRPEGIVILSGP 237
Cdd:NF041000  70 afTYELNEQqiSLRLStvGDFLGRES---------LVIRLLYQLEQIKPQL----FFPEQFQLLKQLLQRRSGLILFSGP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 238 TGSGKSTTLrtasaaY--LEQYGFNdtggillprRRLFTIESPPEGRIPGAIQTAVMDTAQ-GWVDSVKSALRLDPDAIL 314
Cdd:NF041000 137 TGSGKTTTM------YslARKLALN---------KQVITIEDPVEIKEPNFLQLQVNEKAGmTYDTLLKAALRHRPDILI 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446803550 315 NGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERL-EMeGVQARMIAdpQLFIGLLSQRLVQ 379
Cdd:NF041000 202 IGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVIYRLlEL-GISKEELE--QTLIGISYQRLIP 264
PRK10436 PRK10436
hypothetical protein; Provisional
161-441 9.16e-39

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 147.00  E-value: 9.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 161 VPQDARLAerfLKLAGL-FGARYSHYPCVGGLYAVLRLIKDDSQHIpTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTG 239
Cdd:PRK10436 153 LPQDGQFT---VELAGNaYSFRIATLPCRGGEKVVLRLLQQVQQAL-DLETLGMTPAQLAQFRQALQQPQGLILVTGPTG 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 240 SGKSTTLRTAsAAYLEQygfndtggillPRRRLFTIESPPEGRIPGAIQTAVMDTAQGWVDSVKSA-LRLDPDAILNGEI 318
Cdd:PRK10436 229 SGKTVTLYSA-LQTLNT-----------AQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRAlLRQDPDVIMVGEI 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 319 RDHASAITAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADP-QLFIgllSQRLVQVICPHCRLPwhevessrT 397
Cdd:PRK10436 297 RDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASAlKLVI---AQRLVRKLCPHCRQQ--------A 365
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446803550 398 DEERRLVENFCQPDavyLRNHN--GCPHCWRGVNGRTVIAEV--ISPD 441
Cdd:PRK10436 366 SEPIHLPPNIWPGP---LPHWQavGCEHCYHGYYGRTALFEVlpITPV 410
DEXDc smart00487
DEAD-like helicases superfamily;
215-270 1.36e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 42.86  E-value: 1.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 446803550   215 PEQERAVRRMLQRPEGiVILSGPTGSGKSTTLrTASAAYLEQYGFNDTGGILLPRR 270
Cdd:smart00487  11 PYQKEAIEALLSGLRD-VILAAPTGSGKTLAA-LLPALEALKRGKGGRVLVLVPTR 64
 
Name Accession Description Interval E-value
PulE COG2804
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ...
93-441 7.83e-64

Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442055 [Multi-domain]  Cd Length: 561  Bit Score: 216.98  E-value: 7.83e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  93 ISHAATLSASDLHITPGRDSTDFTYleaRVHGELELLDIVRKDEGLELLGATY--SGMtDVikgtqFDPGVPQDARLAer 170
Cdd:COG2804  187 LEDAIKEGASDIHIEPYEKRLRVRF---RIDGVLREVLRLPKSLAPALVSRIKimANL-DI-----AERRLPQDGRIK-- 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 171 fLKLAGL---FgaRYSHYPCVGGLYAVLRLIkDDSQHIPTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTGSGKSTTLR 247
Cdd:COG2804  256 -LRLGGReidL--RVSTLPTVYGEKVVLRIL-DKSAALLDLEQLGFSPDQLERLRRLIRRPHGIILVTGPTGSGKTTTLY 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 248 TAsaayLEQygFNDtggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAQGwvdsVKSALRLDPDAILNGEIRDHA 322
Cdd:COG2804  332 AA----LNE--LNT------PERNIITVEDPVEYQLPGINQVQVnpkigLTFASA----LRSILRQDPDVIMVGEIRDLE 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 323 SAITAIKAAMTGHLMLTTLHANDPINILERL-EMeGVQARMIADPqLfIGLLSQRLVQVICPHCRLPwHEVessrTDEER 401
Cdd:COG2804  396 TAEIAVQAALTGHLVLSTLHTNDAPSAITRLlDM-GVEPFLLASS-L-LGVLAQRLVRRLCPHCKEP-YEP----DPEEL 467
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446803550 402 RLVE-NFCQPDAVYLRNHNGCPHC-WRGVNGRTVIAEVISPD 441
Cdd:COG2804  468 ERLGlPPEELAPLTFYRGVGCEHCnGTGYKGRTGIYELLVID 509
PulE-GspE-like cd01129
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ...
222-378 3.70e-54

PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.


Pssm-ID: 410873 [Multi-domain]  Cd Length: 159  Bit Score: 179.22  E-value: 3.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 222 RRMLQRPEGIVILSGPTGSGKSTTLRtASAAYLEQygfndtggillPRRRLFTIESPPEGRIPGAIQTAVMDTAQ-GWVD 300
Cdd:cd01129    4 RRLIKRPHGLILVTGPTGSGKTTTLY-AMLRELNG-----------PERNIITIEDPVEYQIPGINQSQVNEKIGlTFAD 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446803550 301 SVKSALRLDPDAILNGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADPqlFIGLLSQRLV 378
Cdd:cd01129   72 ALRAILRQDPDIIMVGEIRDAETAEIAIRAALTGHLVLSTLHTNDALGAITRLLDMGIEPFLLASA--LRGVIAQRLV 147
type_II_gspE TIGR02533
type II secretion system protein E; This family describes GspE, the E protein of the type II ...
84-436 5.63e-51

type II secretion system protein E; This family describes GspE, the E protein of the type II secretion system, also called the main terminal branch of the general secretion pathway. This model separates GspE from the PilB protein of type IV pilin biosynthesis. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 131585 [Multi-domain]  Cd Length: 486  Bit Score: 180.65  E-value: 5.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550   84 PVQQKMLGYISHAATLSASDLHITPGRDSTDFTYleaRVHGELEllDIVRKDEGLEllgatySGMTDVIK-GTQFDPG-- 160
Cdd:TIGR02533 107 PVIRLVNSLLSRAVKERASDIHIEPFEKALVVRF---RVDGVLR--DVLSPPKKLH------AALVSRVKiMAKLNIAek 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  161 -VPQDARLAerfLKLAGL-FGARYSHYPCVGGLYAVLRLIKDDSQHIpTFSMLGYHPEQERAVRRMLQRPEGIVILSGPT 238
Cdd:TIGR02533 176 rLPQDGRIS---LRVGGRdIDIRVSTVPTSHGERVVMRLLDKTAVRL-DLETLGMSPELLSRFERLIRRPHGIILVTGPT 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  239 GSGKSTTLRTAsAAYLEQygfndtggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAQGwvdsVKSALRLDPDAI 313
Cdd:TIGR02533 252 GSGKTTTLYAA-LSRLNT-----------PERNILTVEDPVEYQIEGIGQIQVnpkigLTFAAG----LRAILRQDPDII 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  314 LNGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADPQLfiGLLSQRLVQVICPHCRLPWHEve 393
Cdd:TIGR02533 316 MVGEIRDLETAQIAIQASLTGHLVLSTLHTNDAAGAVTRLIDMGVEPFLLASSLL--GVLAQRLVRRLCPHCKEPYEA-- 391
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 446803550  394 ssrTDEERRLVeNFCQPDAVYLRNHNGCPHCWR-GVNGRTVIAE 436
Cdd:TIGR02533 392 ---TPEEIALF-GISPEGPINLYRPVGCPHCNHtGYLGRTGIYE 431
T2SSE pfam00437
Type II/IV secretion system protein; This family contains components of both the Type II ...
93-380 5.65e-48

Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.


Pssm-ID: 425681 [Multi-domain]  Cd Length: 269  Bit Score: 166.69  E-value: 5.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550   93 ISHAATLSASDLHI-TPGRDstdfTYLEARVHGEL-ELLDIvrKDEGLELLGATYSGMTdviKGTQFDPGVPQDARLAER 170
Cdd:pfam00437   4 PLEALDEGASDIHVePPERI----VWIRFRVDGVLrEIPFP--DADALARLISRIKVMA---RLDISERRPPQDGRLPLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  171 FLKLAGLFgaRYSHYPCVGGLYAVLRLIKDDSQHIpTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTGSGKSTTLRTAS 250
Cdd:pfam00437  75 IGGKGVRV--RVSTLPTAGGEKLVIRLLDPSNVAL-SLDELGMTGAQDEALLEFLRQPRGNILVTGPTGSGKTTTLYAAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  251 aayleqyGFNDTggillPRRRLFTIESPPEGRIPGAIQTAV-----MDTAqgwvDSVKSALRLDPDAILNGEIRDHASAI 325
Cdd:pfam00437 152 -------GELNT-----RDENIVTVEDPVEIQLEGINQVQLnaragVTFA----DLLRAILRQDPDRIMVGEIRDLETAE 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446803550  326 TAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADPQLFIglLSQRLVQV 380
Cdd:pfam00437 216 IALQAANTGHLVLSTLHTNSAAGALTRLQDMGVPPFELASSLLLV--IAQRLVRK 268
ATPase_ComGA NF041000
competence type IV pilus ATPase ComGA;
93-379 7.81e-41

competence type IV pilus ATPase ComGA;


Pssm-ID: 468930 [Multi-domain]  Cd Length: 265  Bit Score: 147.59  E-value: 7.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  93 ISHAATLSASDLHITPGRDSTDftyLEARVHGELELLDIVRKDEGLELLgaTY----SGMtdvikgtqfDPG---VPQ-- 163
Cdd:NF041000   4 IEEAIELRASDIHFLPREDGYQ---IKFRIGGGLIPYRELSLEEGQRLI--SYfkflAGM---------DIGekrRPQsg 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 164 --DARLAER--FLKLA--GLFGARYShypcvgglyAVLRLIKDDSQHIPTFsmlgYHPEQERAVRRMLQRPEGIVILSGP 237
Cdd:NF041000  70 afTYELNEQqiSLRLStvGDFLGRES---------LVIRLLYQLEQIKPQL----FFPEQFQLLKQLLQRRSGLILFSGP 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 238 TGSGKSTTLrtasaaY--LEQYGFNdtggillprRRLFTIESPPEGRIPGAIQTAVMDTAQ-GWVDSVKSALRLDPDAIL 314
Cdd:NF041000 137 TGSGKTTTM------YslARKLALN---------KQVITIEDPVEIKEPNFLQLQVNEKAGmTYDTLLKAALRHRPDILI 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446803550 315 NGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERL-EMeGVQARMIAdpQLFIGLLSQRLVQ 379
Cdd:NF041000 202 IGEIRDAETAKAAIRAALTGHLVLSTVHAKSAAGVIYRLlEL-GISKEELE--QTLIGISYQRLIP 264
PRK10436 PRK10436
hypothetical protein; Provisional
161-441 9.16e-39

hypothetical protein; Provisional


Pssm-ID: 236694  Cd Length: 462  Bit Score: 147.00  E-value: 9.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 161 VPQDARLAerfLKLAGL-FGARYSHYPCVGGLYAVLRLIKDDSQHIpTFSMLGYHPEQERAVRRMLQRPEGIVILSGPTG 239
Cdd:PRK10436 153 LPQDGQFT---VELAGNaYSFRIATLPCRGGEKVVLRLLQQVQQAL-DLETLGMTPAQLAQFRQALQQPQGLILVTGPTG 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 240 SGKSTTLRTAsAAYLEQygfndtggillPRRRLFTIESPPEGRIPGAIQTAVMDTAQGWVDSVKSA-LRLDPDAILNGEI 318
Cdd:PRK10436 229 SGKTVTLYSA-LQTLNT-----------AQINICSVEDPVEIPLAGINQTQIHPKAGLTFQRVLRAlLRQDPDVIMVGEI 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 319 RDHASAITAIKAAMTGHLMLTTLHANDPINILERLEMEGVQARMIADP-QLFIgllSQRLVQVICPHCRLPwhevessrT 397
Cdd:PRK10436 297 RDGETAEIAIKAAQTGHLVLSTLHTNSTSETLVRLQQMGIARWMLASAlKLVI---AQRLVRKLCPHCRQQ--------A 365
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446803550 398 DEERRLVENFCQPDavyLRNHN--GCPHCWRGVNGRTVIAEV--ISPD 441
Cdd:PRK10436 366 SEPIHLPPNIWPGP---LPHWQavGCEHCYHGYYGRTALFEVlpITPV 410
PilT COG2805
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ...
93-392 1.76e-38

Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];


Pssm-ID: 442056  Cd Length: 342  Bit Score: 143.31  E-value: 1.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  93 ISHAATLSASDLHITPGRdstdftYLEARVHGELELLD--IVRKDEGLELLGATYS--GMTDVIKGTQFDP--GVPQDAR 166
Cdd:COG2805    9 LKLAVEQGASDLHLTVGS------PPMLRIDGELVPLDdpPLTPEDLEALLKEILTeeQRERLEEEGELDFsySLPGLGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 167 LaerflklaglfgaRYSHYPCVGGLYAVLRLIkddSQHIPTFSMLGYHPEqeraVRRMLQRPEGIVILSGPTGSGKSTTL 246
Cdd:COG2805   83 F-------------RVNIFRQRGGVAAVLRLI---PSEIPTLEELGLPPV----LKELAELPRGLVLVTGPTGSGKSTTL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 247 rtasAAYLEQygFNDTGgillpRRRLFTIESPPEGRIPGA----IQTAV-MDTAqGWVDSVKSALRLDPDAILNGEIRDH 321
Cdd:COG2805  143 ----AAMIDY--INETR-----AKHIITIEDPIEFVHKHKksliNQREVgRDTP-SFANALRAALREDPDVILVGEMRDL 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446803550 322 ASAITAIKAAMTGHLMLTTLHANDPINILERL-----EMEGVQAR-MIAdpQLFIGLLSQRLVQVICPHCRLPWHEV 392
Cdd:COG2805  211 ETIEAALTAAETGHLVFATLHTNSAAQTIDRIidvfpPEEQAQIRsQLA--ESLRGVISQRLLPRADGGGRVAAREI 285
pilT_fam TIGR01420
pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to ...
93-378 2.13e-30

pilus retraction protein PilT; This model represents the PilT subfamily of proteins related to GspE, a protein involved in type II secretion (also called the General Secretion Pathway). PilT is an apparent cytosolic ATPase associated with type IV pilus systems. It is not required for pilin biogenesis, but is required for twitching motility and social gliding behaviors, shown in some species, powered by pilus retraction. Members of this family may be found in some species that type IV pili but have related structures for DNA uptake and natural transformation. [Cell envelope, Surface structures, Cellular processes, Chemotaxis and motility]


Pssm-ID: 273613  Cd Length: 343  Bit Score: 120.89  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550   93 ISHAATLSASDLHITPGrdstdfTYLEARVHGELELLDIVRKDEGlELLGATYSGMTDvikgtqfdpgvpqdaRLAERFL 172
Cdd:TIGR01420   6 LREAVKLGASDIHLTAG------APPAMRIDGDLVRIEFEPLTPE-DTQKLAREILSE---------------KQREEFE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  173 K---------LAGLFGARYSHYPCVGGLYAVLRLIkddSQHIPTFSMLGYHPeqerAVRRMLQRPEGIVILSGPTGSGKS 243
Cdd:TIGR01420  64 EngeldfsfsLPGVGRFRVNAFYQRGGVALVLRLI---PSKIPTFEELGLPP----VLRELAERPRGLILVTGPTGSGKS 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  244 TTLrtasAAYLEQYGFNDTGGILlprrrlfTIESPPEGRIPGA----IQTAV-MDTaQGWVDSVKSALRLDPDAILNGEI 318
Cdd:TIGR01420 137 TTL----ASMIDYINKNKAYHII-------TIEDPIEYVHTNKrsliNQREVgEDT-LSFANALRAALREDPDVILIGEM 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446803550  319 RDHASAITAIKAAMTGHLMLTTLHANDPINILERL-----EMEGVQAR-MIADPqlFIGLLSQRLV 378
Cdd:TIGR01420 205 RDLETVELALTAAETGHLVFGTLHTNSAAQTIERIidvfpAEEQEQIRtQLAES--LVAIISQRLL 268
PilT cd01131
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ...
205-392 3.55e-29

Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.


Pssm-ID: 410875 [Multi-domain]  Cd Length: 223  Bit Score: 114.56  E-value: 3.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 205 IPTFSMLGYHPeqerAVRRMLQRPEGIVILSGPTGSGKSTTLrtasAAYLEQYGFNDTGGILlprrrlfTIESPPEGRIP 284
Cdd:cd01131    1 IPTFEELGLPP----VLKDLALKPRGLVLVTGPTGSGKSTTL----AAMIDYINETRSKHII-------TIEDPIEFVHK 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 285 --GAI--QTAV-MDTAqGWVDSVKSALRLDPDAILNGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERL-----E 354
Cdd:cd01131   66 hkKSLinQREVgRDTE-SFAAALRAALREDPDVILVGEMRDLETIELALTAAETGHLVFSTLHTNSAAQTIDRIidvfpP 144
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446803550 355 MEGVQAR-MIADpqLFIGLLSQRLVQVICPHCRLPWHEV 392
Cdd:cd01131  145 EQQEQVRiQLAS--SLRGVISQRLLPKKDGGGRVAAFEI 181
DotB_TraJ cd19516
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ...
229-378 2.76e-22

dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.


Pssm-ID: 410924 [Multi-domain]  Cd Length: 179  Bit Score: 93.98  E-value: 2.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 229 EGIVILSGPTGSGKSTTLrtasAAYLEQYGFNDTggillPRRRLFTIESPPE---GRIPGA--------IQTAVMDTAQG 297
Cdd:cd19516   11 EGLVYVAGATGSGKSTLL----AAIYRYILENDP-----PDRKIITYEDPIEfvyDGIKSKhsiivqsqIPRHFKSFAKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 298 wvdsVKSALRLDPDAILNGEIRDHASAITAIKAAMTGHLMLTTLHANDPINILERL-------EMEGVQARMIADPQLFI 370
Cdd:cd19516   82 ----VREALRRKPSLIGVGELRDQETISAAVEASLTGHPVYSTVHTKSVAETIRRLislfppeERDAAAYDLLSTLRFII 157

                 ....*...
gi 446803550 371 gllSQRLV 378
Cdd:cd19516  158 ---VQRLV 162
PilU COG5008
Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];
193-378 1.37e-21

Type IV pilus assembly protein, ATPase PilU [Cell motility, Extracellular structures];


Pssm-ID: 444032  Cd Length: 370  Bit Score: 96.32  E-value: 1.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 193 AVLRLIKDDsqhIPTFSMLGYhPE--QERAvrrMLQRpeGIVILSGPTGSGKSTTLrtasAAYLEQYGFNDTGGILlprr 270
Cdd:COG5008   94 MVLRRIETE---IPTLDELGL-PPvlKDLI---MEKR--GLVLFVGATGSGKSTTL----AAMIDHRNENSSGHIL---- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 271 rlfTIESPPE------GRIpgAIQTAV-MDTaQGWVDSVKSALRLDPDAILNGEIRDHASAITAIKAAMTGHLMLTTLHA 343
Cdd:COG5008  157 ---TIEDPIEfvhkhkKSI--VTQREVgVDT-ESYEVALKNALRQAPDVILIGEIRDRETMEHAIAFAETGHLCLATLHA 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446803550 344 NDpinilerlemeGVQA--RMI------ADPQLFIGL-------LSQRLV 378
Cdd:COG5008  231 NN-----------ANQAldRIInffpeeRRPQLLMDLslnlraiVSQRLV 269
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
217-365 4.22e-18

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 81.82  E-value: 4.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 217 QERAVRRMLQRPEGIVIlSGPTGSGKSTTLRTASAAyleqygfndtggiLLPRRRLFTIESPPEGRIP-----------G 285
Cdd:cd01130    1 MAAFLRLAVRARKNILI-SGGTGSGKTTLLNALLSF-------------IPPDERIVTIEDTRELQLPhpnvvhlltrpG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 286 AIQTAVMDTAqgwvDSVKSALRLDPDAILNGEIRDHAsAITAIKAAMTGHL-MLTTLHANDPINILERLEMEGVQARMIA 364
Cdd:cd01130   67 GGEKGEVTMA----DLLKAALRMRPDRIIVGEVRGGE-AYDMLQAMNTGHPgSITTIHANSAEDAIDRLATLVLEAGVNL 141

                 .
gi 446803550 365 D 365
Cdd:cd01130  142 D 142
type_II_IV_secretion_ATPases cd19477
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ...
220-381 8.49e-17

type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410885 [Multi-domain]  Cd Length: 168  Bit Score: 77.82  E-value: 8.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 220 AVRRMLQRPeGIVILSGPTGSGKSTTLRtasaAYLEQygfndtggiLLPRRRLFTIESPPEGRIP---GAIQTAVmDTAQ 296
Cdd:cd19477    2 AIKDGIAIG-KNVIVCGGTGSGKTTYIK----SILEF---------IPKEERIISIEDTEEIVFKhhkNYTQLFF-GGNI 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 297 GWVDSVKSALRLDPDAILNGEIRDhASAITAIKAAMTGH-LMLTTLHANDPINILERLEMEGVQ---ARMI---ADPQLF 369
Cdd:cd19477   67 TSADCLKSCLRQRPDRIILGELRS-SEAYDFYNVLCSGHkGTLTTLHAGSSEEAFIRLAN*SSSnsaARNIkfeSLIEGF 145
                        170
                 ....*....|....*.
gi 446803550 370 ----IGLLSQRLVQVI 381
Cdd:cd19477  146 kdliDGIVHINHHKQC 161
plasmid_TraJ TIGR02525
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ...
195-353 4.76e-14

plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524). [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 131577 [Multi-domain]  Cd Length: 372  Bit Score: 73.69  E-value: 4.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  195 LRLIKDDsqhIPTFSMLGYHPEQERAVRRMlqrpEGIVILSGPTGSGKSTTLrtasAAYLEQYGFNDtggillPRRRLFT 274
Cdd:TIGR02525 122 LRVIPSD---IPDLKQMGIEPDLFNSLLPA----AGLGLICGETGSGKSTLA----ASIYQHCGETY------PDRKIVT 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  275 IESPPEGRI--PGAI----QTAVMDTAQGWVDSVKSALRLDPDAILNGEIRDHASAITAIKAAMTGHLMLTTLHANDPIN 348
Cdd:TIGR02525 185 YEDPIEYILgsPDDLlppaQSQIGRDVDSFANGIRLALRRAPKIIGVGEIRDLETFQAAVLAGQSGHFCLGTLHVKSPGE 264

                  ....*
gi 446803550  349 ILERL 353
Cdd:TIGR02525 265 AISRC 269
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
232-356 2.04e-13

Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440395 [Multi-domain]  Cd Length: 462  Bit Score: 72.04  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 232 VILSGPTGSGKSTTLrtasaayleqygfndtGGILL---PRRRLFTIESPPEGRIPG--AIQTAVMDTAQGWV------D 300
Cdd:COG0630  293 VLVAGGTASGKTTLL----------------NALLSfipPDAKIVTIEDTRELNLPHenWISLVTRESFGGEEgdvtmfD 356
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446803550 301 SVKSALRLDPDAILNGEIRDhASAITAIKAAMTGHLMLTTLHANDPINILERLEME 356
Cdd:COG0630  357 LLKAALRQRPDYIVVGEVRG-EEAYTLFQAMATGHGVLSTFHADSVESAINRLTSP 411
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
232-362 6.53e-12

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 67.11  E-value: 6.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 232 VILSGPTGSGKSTTLRTASAAyleqygfndtggiLLPRRRLFTIESPPEGRIP-----------------GAIQTAvmdt 294
Cdd:COG4962  185 ILVSGGTGSGKTTLLNALSGF-------------IPPDERIVTIEDAAELQLQhphvvrletrppnvegaGEVTLR---- 247
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446803550 295 aqgwvDSVKSALRLDPDAILNGEIRDhASAITAIKAAMTGHL-MLTTLHANDPINILERLEMEGVQARM 362
Cdd:COG4962  248 -----DLVRNALRMRPDRIIVGEVRG-AEALDMLQAMNTGHDgSMSTLHANSARDALARLETLALMAGE 310
PRK13833 PRK13833
conjugal transfer protein TrbB; Provisional
217-354 2.76e-10

conjugal transfer protein TrbB; Provisional


Pssm-ID: 172360 [Multi-domain]  Cd Length: 323  Bit Score: 61.74  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 217 QERAVRRMLQRPEGIVIlSGPTGSGKSTTLRTASAAYLEQygfndtggilLPRRRLFTIESPPEgrIPGAIQTAVMDTAQ 296
Cdd:PRK13833 133 QASVIRSAIDSRLNIVI-SGGTGSGKTTLANAVIAEIVAS----------APEDRLVILEDTAE--IQCAAENAVALHTS 199
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446803550 297 GWVDS---VKSALRLDPDAILNGEIRDHAsAITAIKAAMTGHL-MLTTLHANDPINILERLE 354
Cdd:PRK13833 200 DTVDMarlLKSTMRLRPDRIIVGEVRDGA-ALTLLKAWNTGHPgGVTTIHSNTAMSALRRLE 260
PRK13851 PRK13851
type IV secretion system protein VirB11; Provisional
232-353 1.32e-07

type IV secretion system protein VirB11; Provisional


Pssm-ID: 172375  Cd Length: 344  Bit Score: 53.36  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 232 VILSGPTGSGKSTTLRTASAAyleqygfndtggiLLPRRRLFTIESPPEGRIPGAIQTAVMDTAQGW----VDS---VKS 304
Cdd:PRK13851 165 MLLCGPTGSGKTTMSKTLISA-------------IPPQERLITIEDTLELVIPHENHVRLLYSKNGAglgaVTAehlLQA 231
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446803550 305 ALRLDPDAILNGEIRDHAsAITAIKAAMTGHL-MLTTLHANDPINILERL 353
Cdd:PRK13851 232 SLRMRPDRILLGEMRDDA-AWAYLSEVVSGHPgSISTIHGANPVQGFKKL 280
PRK13894 PRK13894
conjugal transfer ATPase TrbB; Provisional
215-355 1.41e-07

conjugal transfer ATPase TrbB; Provisional


Pssm-ID: 184377  Cd Length: 319  Bit Score: 53.20  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 215 PEQERAVRRMLQRPEGIVILSGpTGSGKsTTLrtASAAYLEQYGFNdtggillPRRRLFTIESPpegripGAIQTAVMDT 294
Cdd:PRK13894 135 AAQREAIIAAVRAHRNILVIGG-TGSGK-TTL--VNAIINEMVIQD-------PTERVFIIEDT------GEIQCAAENY 197
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 295 AQgWVDSV--------KSALRLDPDAILNGEIRDhASAITAIKAAMTGHL-MLTTLHANDPINILERLEM 355
Cdd:PRK13894 198 VQ-YHTSIdvnmtallKTTLRMRPDRILVGEVRG-PEALDLLMAWNTGHEgGAATLHANNAKAGLDRLKS 265
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
215-368 4.11e-07

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 50.26  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  215 PEQERAVRRMLQRPEGIVILSGPTGSGKSTTLRTASAAYlEQYGFndtggillprrrlftiesPPEGRIPGAIQTAVM-- 292
Cdd:pfam13604   4 AEQAAAVRALLTSGDRVAVLVGPAGTGKTTALKALREAW-EAAGY------------------RVIGLAPTGRAAKVLge 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550  293 ------DTAQGWVDSVKSALRLDPDAILngeIRDHASaitaikaamtghlMLTTLHANDpinILERLEMEGVQARMIADP 366
Cdd:pfam13604  65 elgipaDTIAKLLHRLGGRAGLDPGTLL---IVDEAG-------------MVGTRQMAR---LLKLAEDAGARVILVGDP 125

                  ...
gi 446803550  367 -QL 368
Cdd:pfam13604 126 rQL 128
PRK13900 PRK13900
type IV secretion system ATPase VirB11; Provisional
232-360 1.31e-05

type IV secretion system ATPase VirB11; Provisional


Pssm-ID: 184381  Cd Length: 332  Bit Score: 47.06  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 232 VILSGPTGSGKSTtlrtasaayleqygFNDTGGILLPRR-RLFTIESPPE---GRIPGAIQTAVMDTAQGWV-----DSV 302
Cdd:PRK13900 163 IIISGGTSTGKTT--------------FTNAALREIPAIeRLITVEDAREivlSNHPNRVHLLASKGGQGRAkvttqDLI 228
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446803550 303 KSALRLDPDAILNGEIRDhASAITAIKAAMTGHL-MLTTLHANDPINILERLEMEGVQA 360
Cdd:PRK13900 229 EACLRLRPDRIIVGELRG-AEAFSFLRAINTGHPgSISTLHADSPAMAIEQLKLMVMQA 286
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
215-256 9.78e-05

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 44.97  E-value: 9.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446803550 215 PEQERAVRRMLQRpEGIVILSGPTGSGKSTTLRTASAAYLEQ 256
Cdd:COG0507  127 DEQREAVALALTT-RRVSVLTGGAGTGKTTTLRALLAALEAL 167
DEXDc smart00487
DEAD-like helicases superfamily;
215-270 1.36e-04

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 42.86  E-value: 1.36e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 446803550   215 PEQERAVRRMLQRPEGiVILSGPTGSGKSTTLrTASAAYLEQYGFNDTGGILLPRR 270
Cdd:smart00487  11 PYQKEAIEALLSGLRD-VILAAPTGSGKTLAA-LLPALEALKRGKGGRVLVLVPTR 64
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
216-253 2.07e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 38.69  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446803550 216 EQERAVRRMLQRPegIVILSGPTGSGKSTTLRTASAAY 253
Cdd:cd17933    1 EQKAAVRLVLRNR--VSVLTGGAGTGKTTTLKALLAAL 36
AAA_19 pfam13245
AAA domain;
217-271 3.00e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 37.97  E-value: 3.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446803550  217 QERAVRRMLQRPegIVILSGPTGSGKSTTLRTASAAYLEQYGFNDTGGILLPRRR 271
Cdd:pfam13245   1 QREAVRTALPSK--VVLLTGGPGTGKTTTIRHIVALLVALGGVSFPILLAAPTGR 53
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
167-255 3.52e-03

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 39.84  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 167 LAERFLklAGLFGAR--YSHYPCVGGlYAVLRLIKDDSQH----------IPTFSMLGYHPEQ--ERAVRRMLQRPEG-I 231
Cdd:cd14879   10 LASRFR--SDLPYTRlgSSALVAVNP-YKYLSSNSDASLGeygseyydttSGSKEPLPPHAYDlaARAYLRMRRRSEDqA 86
                         90       100
                 ....*....|....*....|....
gi 446803550 232 VILSGPTGSGKSTTLRTASAAYLE 255
Cdd:cd14879   87 VVFLGETGSGKSESRRLLLRQLLR 110
PTZ00202 PTZ00202
tuzin; Provisional
171-249 4.37e-03

tuzin; Provisional


Pssm-ID: 240312  Cd Length: 550  Bit Score: 39.77  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446803550 171 FLKLAGLFGARYSHYPCVGGLY----AVLRLIKDDSQHIPTFSMLGYHPEQ-------ERAVRRMLQRPEG----IVILS 235
Cdd:PTZ00202 213 LLGVASVFGWNFKNYRTQQRSYqlkvAVSTLTQPLNPRPSTLQSAPAVIRQfvsreaeESWVRQVLRRLDTahprIVVFT 292
                         90
                 ....*....|....
gi 446803550 236 GPTGSGKSTTLRTA 249
Cdd:PTZ00202 293 GFRGCGKSSLCRSA 306
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
231-268 7.39e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.08  E-value: 7.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446803550 231 IVILSGPTGSGKSTTLRTASaaylEQYGFN--DTGGILLP 268
Cdd:cd02020    1 IIAIDGPAGSGKSTVAKLLA----KKLGLPylDTGGIRTE 36
DEXDc2 smart00488
DEAD-like helicases superfamily;
213-258 8.49e-03

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 38.13  E-value: 8.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 446803550   213 YHPEQE---RAVRRMLQRpEGIVILSGPTGSGKSTTLRTASAAYLEQYG 258
Cdd:smart00488   9 PYPIQYefmEELKRVLDR-GKIGILESPTGTGKTLSLLCLTLTWLRSFP 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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