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Conserved domains on  [gi|515933375|ref|WP_017363958|]
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MULTISPECIES: SPOR domain-containing protein [Pseudomonadaceae]

Protein Classification

SPOR domain-containing protein( domain architecture ID 11459733)

SPOR domain-containing protein similar to Bacillus subtilis stage II sporulation protein B and Escherichia coli cell division proteins FtsN, DamX, and DedD

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
59-201 1.07e-24

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 94.07  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  59 PAEVVEPEQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQPSAPEQAKTEQSVATASAKPEGRldannlpisWSVQLASL 138
Cdd:COG3147    3 EEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAAAAPAAKAAAPAGGG---------WVVQLGAF 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515933375 139 SSRGGAENLQKTLRSQGYNAYIRTFDG----MNRVFVGPLIERAEAERLRDQLNRQHKLSGFVVRFQ 201
Cdd:COG3147   74 SNEDNAKELVAKLRAAGYPAYTEPVTTgggtLYRVRVGPFASRAEAEAALAKLKKLTGLKGFVVRYK 140
 
Name Accession Description Interval E-value
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
59-201 1.07e-24

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 94.07  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  59 PAEVVEPEQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQPSAPEQAKTEQSVATASAKPEGRldannlpisWSVQLASL 138
Cdd:COG3147    3 EEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAAAAPAAKAAAPAGGG---------WVVQLGAF 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515933375 139 SSRGGAENLQKTLRSQGYNAYIRTFDG----MNRVFVGPLIERAEAERLRDQLNRQHKLSGFVVRFQ 201
Cdd:COG3147   74 SNEDNAKELVAKLRAAGYPAYTEPVTTgggtLYRVRVGPFASRAEAEAALAKLKKLTGLKGFVVRYK 140
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
131-199 3.00e-15

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 67.77  E-value: 3.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515933375  131 WSVQLASLSSRGGAENLQKTLRSQGYNAYIRTF---DGMNRVFVGPLIERAEAERLRDQLNRQHKLSGFVVR 199
Cdd:pfam05036   5 YYVQLGAFSNEANAEALAAKLRAKGFAAYVAVTskgGGLYRVRVGPFASREEARAALKKLKALAGLSPFVVK 76
PRK12757 PRK12757
cell division protein FtsN; Provisional
85-187 1.55e-06

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 47.34  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  85 VPEQPKQAPVPAVQPSAPEQAKTEQSVATASAKPEGRldannlpisWSVQLASLSSRGGAENLQKTLRSQGYNAYIRTFD 164
Cdd:PRK12757 148 APVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQR---------WMVQCGSFKGTEQAESVRAQLAFAGIESRITTGG 218
                         90       100
                 ....*....|....*....|...
gi 515933375 165 GMNRVFVGPLIERAEAERLRDQL 187
Cdd:PRK12757 219 GWNRVVLGPYNSKAAADKMLQRL 241
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
33-199 8.36e-06

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 45.45  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375   33 EDEMRRVVVEAPAMPQAPAATEIVVEPAEVVEPEQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQPSAPEQAKTEQSVA 112
Cdd:TIGR02223 139 APSEQTVAVEARKQTAEKKPQKARTAEAQKTPVETEKIASKVKEAKQKQKALPKQTAETQSNSKPIETAPKADKADKTKP 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  113 TASAKPEGRldannlpisWSVQLASLSSRGGAENLQKTLRSQGYNAYIRTFDG--MNRVFVGPLIERAEAERLRDQLNRq 190
Cdd:TIGR02223 219 KPKEKAERA---------AALQCGAYANKEQAESVRAKLAFLGISSKITTTDGgkWYRVVSGPYKNKDDAEKDLNKLKV- 288

                  ....*....
gi 515933375  191 HKLSGFVVR 199
Cdd:TIGR02223 289 AGVAGCIIN 297
 
Name Accession Description Interval E-value
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
59-201 1.07e-24

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 94.07  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  59 PAEVVEPEQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQPSAPEQAKTEQSVATASAKPEGRldannlpisWSVQLASL 138
Cdd:COG3147    3 EEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAAAAPAAKAAAPAGGG---------WVVQLGAF 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515933375 139 SSRGGAENLQKTLRSQGYNAYIRTFDG----MNRVFVGPLIERAEAERLRDQLNRQHKLSGFVVRFQ 201
Cdd:COG3147   74 SNEDNAKELVAKLRAAGYPAYTEPVTTgggtLYRVRVGPFASRAEAEAALAKLKKLTGLKGFVVRYK 140
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
131-199 3.00e-15

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 67.77  E-value: 3.00e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515933375  131 WSVQLASLSSRGGAENLQKTLRSQGYNAYIRTF---DGMNRVFVGPLIERAEAERLRDQLNRQHKLSGFVVR 199
Cdd:pfam05036   5 YYVQLGAFSNEANAEALAAKLRAKGFAAYVAVTskgGGLYRVRVGPFASREEARAALKKLKALAGLSPFVVK 76
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
31-199 1.95e-10

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 57.71  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  31 SREDEMRRVVVEAPAMPQAPAATEIVVEPAEVVEPEQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQPSAPEQAKTEQS 110
Cdd:COG3087   25 AAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAAALAAASAAAAAAAAPAAAAAEAA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375 111 VATASAKPEGRLDANNLPISWSVQLASLSSRGGAENLQKTLRSQGYNAYIRTFD----GMNRVFVGPLIERAEAERLRDQ 186
Cdd:COG3087  105 AAPAGMAKKEAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLGLEARVVEVEvgggTWYRVRVGPFSSRAEAEKAREK 184
                        170
                 ....*....|...
gi 515933375 187 LnRQHKLSGFVVR 199
Cdd:COG3087  185 L-KAAGIDALVVR 196
PRK12757 PRK12757
cell division protein FtsN; Provisional
85-187 1.55e-06

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 47.34  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  85 VPEQPKQAPVPAVQPSAPEQAKTEQSVATASAKPEGRldannlpisWSVQLASLSSRGGAENLQKTLRSQGYNAYIRTFD 164
Cdd:PRK12757 148 APVQPQTPAPVRTQPAAPVTQAVEAPKVEAEKEKEQR---------WMVQCGSFKGTEQAESVRAQLAFAGIESRITTGG 218
                         90       100
                 ....*....|....*....|...
gi 515933375 165 GMNRVFVGPLIERAEAERLRDQL 187
Cdd:PRK12757 219 GWNRVVLGPYNSKAAADKMLQRL 241
PRK10927 PRK10927
cell division protein FtsN;
85-181 2.79e-06

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 46.60  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  85 VPEQPKQAPVPAVQpSAPEQAKTEQSVATASAKPEGRL------------DANNLPIS-----------------WSVQL 135
Cdd:PRK10927 174 TTEQSWQQQTRTSQ-AAPVQAQPRQSKPASTQQPYQDLlqtpahttaqskPQQAAPVTraadapkptaekkderrWMVQC 252
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515933375 136 ASLSSRGGAENLQKTLRSQGYNAYIRTFDGMNRVFVGPLIERAEAE 181
Cdd:PRK10927 253 GSFRGAEQAETVRAQLAFEGFDSKITTNNGWNRVVIGPVKGKENAD 298
PRK11633 PRK11633
cell division protein DedD; Provisional
11-202 3.91e-06

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 45.76  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  11 RMVGALVLVALAVIFLPMLL----------------------SREDEMRRVVVEAPAMPQAPAATEIVV---EPAEVVEP 65
Cdd:PRK11633   8 RLVGTIVLVALGVIVLPGLLdgqkkhyqdefaaiplvpkpgdRDEPDMMPAATQALPTQPPEGAAEAVRagdAAAPSLDP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  66 EQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQP-----SAPEQAKTEQSVATASAKPEGRldannlpiSWSVQLASLSS 140
Cdd:PRK11633  88 ATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPqqkveAPPAPKPEPKPVVEEKAAPTGK--------AYVVQLGALKN 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515933375 141 RGGAENLQKTLRSQGYNAYI---RTFDG-MNRVFVGPLIERAEAERLRDQLNRQHKLSGFVVRFQP 202
Cdd:PRK11633 160 ADKVNEIVAKLRLSGYRVYTvpsTPVQGkITRIYVGPDASKDKLKGSLGELKQLSGLSGVVMGYTP 225
ftsN TIGR02223
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ...
33-199 8.36e-06

cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]


Pssm-ID: 274041 [Multi-domain]  Cd Length: 298  Bit Score: 45.45  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375   33 EDEMRRVVVEAPAMPQAPAATEIVVEPAEVVEPEQLPQEPVPVEEVEPQIVEVPEQPKQAPVPAVQPSAPEQAKTEQSVA 112
Cdd:TIGR02223 139 APSEQTVAVEARKQTAEKKPQKARTAEAQKTPVETEKIASKVKEAKQKQKALPKQTAETQSNSKPIETAPKADKADKTKP 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  113 TASAKPEGRldannlpisWSVQLASLSSRGGAENLQKTLRSQGYNAYIRTFDG--MNRVFVGPLIERAEAERLRDQLNRq 190
Cdd:TIGR02223 219 KPKEKAERA---------AALQCGAYANKEQAESVRAKLAFLGISSKITTTDGgkWYRVVSGPYKNKDDAEKDLNKLKV- 288

                  ....*....
gi 515933375  191 HKLSGFVVR 199
Cdd:TIGR02223 289 AGVAGCIIN 297
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
82-198 1.73e-05

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 44.28  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515933375  82 IVEVPEQPKQAPVPAvqPSAPEQAKTEQSVATASAKPEGrldannlpisWSVQLASLSSRGGAENLQKTLRSQ-GYNAYI 160
Cdd:PRK10672 253 VLEGSEPTPTAPSSA--PATAPAAAAPQAAATSSSASGN----------FVVQVGAVSDQQRAQQWQQSLSQRfGVPGRV 320
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515933375 161 RTFDGMNRVFVGPLIERAEAERLRDQLNRQHKLSGFVV 198
Cdd:PRK10672 321 TQNGAVYRVQLGPFASRQQASALQQRLQTEAQQQSFIT 358
 
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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