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Conserved domains on  [gi|1005571654|ref|WP_061664895|]
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MULTISPECIES: spore coat assembly protein ExsA [Bacillus]

Protein Classification

C40 family peptidase( domain architecture ID 13493263)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 6-49 2.48e-17

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


:

Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 75.60  E-value: 2.48e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1005571654   6 VQKGDTLWKIAKKYGVDFDTLKKTNTQLSNPDLIMPGMKIKVPS 49
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIYPGMKIKIPS 44
PRK13914 super family cl36314
invasion associated endopeptidase;
5-150 1.20e-05

invasion associated endopeptidase;


The actual alignment was detected with superfamily member PRK13914:

Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.26  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654   5 IVQKGDTLWKIAKKYGVDFDTLKKTNTQLSnpDLIMPGMKIKVPSKSVHMKQQAG---------AGSAPPKQYVKEVQQK 75
Cdd:PRK13914   31 VVEAGDTLWGIAQSKGTTVDAIKKANNLTT--DKIVPGQKLQVNEVAAAEKTEKSvsatwlnvrSGAGVDNSIITSIKGG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  76 efaatpTPLGIEDEE-----EVTYQ-----------------SAPITQQPAMQQTQKEVQIKPQKEMQVKPQKEVQVKPQ 133
Cdd:PRK13914  109 ------TKVTVETTEsngwhKITYNdgktgfvngkyltdkvtSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTP 182

                         170
                  ....*....|....*..
gi 1005571654 134 kemqvKPQKEVQKEQPI 150
Cdd:PRK13914  183 -----APKVAETKETPV 194
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 469-579 1.32e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  469 PNMMPYQMPYQQPMMPPNPYY-QQPNPYQMPYQQgapfgPQHTSMPNQNMMPMDNNMPPLVQGEedcgcggesrlyspQP 547
Cdd:PRK10263   747 PIVEPVQQPQQPVAPQQQYQQpQQPVAPQPQYQQ-----PQQPVAPQPQYQQPQQPVAPQPQYQ--------------QP 807

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1005571654  548 GGPQYANPLYYQPTQSAyAPQPgtMYYQPDPP 579
Cdd:PRK10263   808 QQPVAPQPQYQQPQQPV-APQP--QYQQPQQP 836
 
Name Accession Description Interval E-value
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 6-49 2.48e-17

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 75.60  E-value: 2.48e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1005571654   6 VQKGDTLWKIAKKYGVDFDTLKKTNTQLSNPDLIMPGMKIKVPS 49
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIYPGMKIKIPS 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 2-47 1.69e-14

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 67.51  E-value: 1.69e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1005571654   2 KIHIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNPDLIMPGMKIKV 47
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAAN-PLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-50 6.40e-14

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 69.74  E-value: 6.40e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1005571654   1 MKIHIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNpDLIMPGMKIKVPSK 50
Cdd:COG1388   109 PVTYTVKKGDTLWSIARRYGVSVEELKRWN-GLSS-DTIRPGQKLKIPAS 156
LysM smart00257
Lysin motif;
3-47 2.24e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.69  E-value: 2.24e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1005571654    3 IHIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNPDLIMPGMKIKV 47
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELN-NILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 4-48 4.80e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 60.49  E-value: 4.80e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1005571654   4 HIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNPDlIMPGMKIKVP 48
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPN-LYVGQKLKIP 43
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 4-48 3.53e-06

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 46.83  E-value: 3.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1005571654   4 HIVQKGDTLWKIAKKY---GVDFDTLKKTNTQ-LSNPDLIMPGMKIKVP 48
Cdd:PRK11198   98 YTVKSGDTLSAIAKKVygnANKYNKIFEANKPmLKSPDKIYPGQVLRIP 146
PRK13914 PRK13914
invasion associated endopeptidase;
5-150 1.20e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.26  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654   5 IVQKGDTLWKIAKKYGVDFDTLKKTNTQLSnpDLIMPGMKIKVPSKSVHMKQQAG---------AGSAPPKQYVKEVQQK 75
Cdd:PRK13914   31 VVEAGDTLWGIAQSKGTTVDAIKKANNLTT--DKIVPGQKLQVNEVAAAEKTEKSvsatwlnvrSGAGVDNSIITSIKGG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  76 efaatpTPLGIEDEE-----EVTYQ-----------------SAPITQQPAMQQTQKEVQIKPQKEMQVKPQKEVQVKPQ 133
Cdd:PRK13914  109 ------TKVTVETTEsngwhKITYNdgktgfvngkyltdkvtSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTP 182

                         170
                  ....*....|....*..
gi 1005571654 134 kemqvKPQKEVQKEQPI 150
Cdd:PRK13914  183 -----APKVAETKETPV 194
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 469-579 1.32e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  469 PNMMPYQMPYQQPMMPPNPYY-QQPNPYQMPYQQgapfgPQHTSMPNQNMMPMDNNMPPLVQGEedcgcggesrlyspQP 547
Cdd:PRK10263   747 PIVEPVQQPQQPVAPQQQYQQpQQPVAPQPQYQQ-----PQQPVAPQPQYQQPQQPVAPQPQYQ--------------QP 807

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1005571654  548 GGPQYANPLYYQPTQSAyAPQPgtMYYQPDPP 579
Cdd:PRK10263   808 QQPVAPQPQYQQPQQPV-APQP--QYQQPQQP 836
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 88-180 1.34e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.37  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  88 DEEEVTYQSAPITQQ-----PAMQQTQKEVQIKPQKEMQVKPQKEVQVKPQKEM----QVKPQKEVQKEQPIQKEKPVEK 158
Cdd:TIGR02794  44 DPGAVAQQANRIQQQkkpaaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRaaaeKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100
                  ....*....|....*....|..
gi 1005571654 159 PSVIQKPpviEKQKPAEKENTK 180
Cdd:TIGR02794 124 AKAKQAA---EAKAKAEAEAER 142
 
Name Accession Description Interval E-value
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 6-49 2.48e-17

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 75.60  E-value: 2.48e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1005571654   6 VQKGDTLWKIAKKYGVDFDTLKKTNTQLSNPDLIMPGMKIKVPS 49
Cdd:TIGR02899   1 VQKGDTLWKIAKKYGVDFDELIQANPQLSNPNLIYPGMKIKIPS 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 2-47 1.69e-14

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 67.51  E-value: 1.69e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1005571654   2 KIHIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNPDLIMPGMKIKV 47
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAAN-PLINPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-50 6.40e-14

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 69.74  E-value: 6.40e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1005571654   1 MKIHIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNpDLIMPGMKIKVPSK 50
Cdd:COG1388   109 PVTYTVKKGDTLWSIARRYGVSVEELKRWN-GLSS-DTIRPGQKLKIPAS 156
LysM smart00257
Lysin motif;
3-47 2.24e-12

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 61.69  E-value: 2.24e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1005571654    3 IHIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNPDLIMPGMKIKV 47
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELN-NILDPDNLQVGQKLKI 44
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 2-51 3.59e-12

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 64.64  E-value: 3.59e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1005571654   2 KIHIVQKGDTLWKIAKKY---GVDFDTLKKTNT-QLSNPDLIMPGMKIKVPSKS 51
Cdd:COG1652   110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEANRdQIKNPDLIYPGQVLRIPALE 163
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 4-48 4.80e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 60.49  E-value: 4.80e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1005571654   4 HIVQKGDTLWKIAKKYGVDFDTLKKTNtQLSNPDlIMPGMKIKVP 48
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELN-GLSSPN-LYVGQKLKIP 43
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 4-48 3.53e-06

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 46.83  E-value: 3.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1005571654   4 HIVQKGDTLWKIAKKY---GVDFDTLKKTNTQ-LSNPDLIMPGMKIKVP 48
Cdd:PRK11198   98 YTVKSGDTLSAIAKKVygnANKYNKIFEANKPmLKSPDKIYPGQVLRIP 146
PRK13914 PRK13914
invasion associated endopeptidase;
5-150 1.20e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.26  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654   5 IVQKGDTLWKIAKKYGVDFDTLKKTNTQLSnpDLIMPGMKIKVPSKSVHMKQQAG---------AGSAPPKQYVKEVQQK 75
Cdd:PRK13914   31 VVEAGDTLWGIAQSKGTTVDAIKKANNLTT--DKIVPGQKLQVNEVAAAEKTEKSvsatwlnvrSGAGVDNSIITSIKGG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  76 efaatpTPLGIEDEE-----EVTYQ-----------------SAPITQQPAMQQTQKEVQIKPQKEMQVKPQKEVQVKPQ 133
Cdd:PRK13914  109 ------TKVTVETTEsngwhKITYNdgktgfvngkyltdkvtSTPVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTP 182

                         170
                  ....*....|....*..
gi 1005571654 134 kemqvKPQKEVQKEQPI 150
Cdd:PRK13914  183 -----APKVAETKETPV 194
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-51 4.00e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 46.61  E-value: 4.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1005571654   2 KIHIVQKGDTLWKIAKKYGVDFDTLKKTNTQLSnpDLIMPGMKIKVPSKS 51
Cdd:PRK06347  331 KIYTVVKGDSLWRIANNHKVTVANLKAWNNLKS--DFIYPGQKLKVSAGS 378
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-52 5.64e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 46.23  E-value: 5.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1005571654   2 KIHIVQKGDTLWKIAKKYGVDFDTLKKTNTQLSnpDLIMPGMKIKVPSKSV 52
Cdd:PRK06347  480 KVYTVAKGDSLWRIANNNKVTIANLKSWNNLKS--DFIYPGQKLKVSAGST 528
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-51 6.82e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 45.84  E-value: 6.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1005571654   2 KIHIVQKGDTLWKIAKKYGVDFDTLKKTNTQLSnpDLIMPGMKIKVPSKS 51
Cdd:PRK06347  406 KVYTVVKGDSLWRIANNNKVTIANLKSWNNLKS--DFIYPGQKLKVSAGS 453
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 469-579 1.32e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  469 PNMMPYQMPYQQPMMPPNPYY-QQPNPYQMPYQQgapfgPQHTSMPNQNMMPMDNNMPPLVQGEedcgcggesrlyspQP 547
Cdd:PRK10263   747 PIVEPVQQPQQPVAPQQQYQQpQQPVAPQPQYQQ-----PQQPVAPQPQYQQPQQPVAPQPQYQ--------------QP 807

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1005571654  548 GGPQYANPLYYQPTQSAyAPQPgtMYYQPDPP 579
Cdd:PRK10263   808 QQPVAPQPQYQQPQQPV-APQP--QYQQPQQP 836
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 484-585 1.48e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.08  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  484 PPNPYYQQPN-PYQMPYQQGAPFGPQHTSmpnqnmmPMDNNMPPLVQGEEDCGCGGESRLYSPQPGGPQYANPLYYQPTQ 562
Cdd:PRK10263   381 PQQSQYAQPAvQYNEPLQQPVQPQQPYYA-------PAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQ 453

                           90       100
                   ....*....|....*....|...
gi 1005571654  563 SAYAPQPGTMYYQPDPPNVFGEP 585
Cdd:PRK10263   454 STFAPQSTYQTEQTYQQPAAQEP 476
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 421-527 7.59e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  421 PNIMPIMDNNQMPNMMPIMDNNQMPNIMPIMDNNQMPNMMPIMDNNQPPNMMPYQMPYQQPMMP--PNPYYQQPN----- 493
Cdd:PRK10263   747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPvaPQPQYQQPQqpvap 826

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1005571654  494 --PYQMPYQQGAPfGPQHT-----SMPNQNMMPMDNNMPPL 527
Cdd:PRK10263   827 qpQYQQPQQPVAP-QPQDTllhplLMRNGDSRPLHKPTTPL 866
PRK13914 PRK13914
invasion associated endopeptidase;
4-104 7.85e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.10  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654   4 HIVQKGDTLWKIAKKYGVDFDTLKKTNTQLSNPDLIMPGMKIKVPSKSVHMKQQAGA-GSAPPKQYVKEVQQKEFAATPT 82
Cdd:PRK13914  202 HAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKTeAPAAEKQAAPVVKENTNTNTAT 281

                          90       100
                  ....*....|....*....|..
gi 1005571654  83 plgiEDEEEVTYQSAPITQQPA 104
Cdd:PRK13914  282 ----TEKKETTTQQQTAPKAPT 299
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 469-579 1.14e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  469 PNMMPYQMPYQQPMMPPNPYYQQPNPYQMPYQQGAPFGPQHTSMPNQNMMPMDNNMPPLVQGEEDCGcggeSRLYSPQPG 548
Cdd:PRK10263   377 PEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVA----GNAWQAEEQ 452

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1005571654  549 GPQYANPLYYQPTQSAYAPQPGTMYYQPDPP 579
Cdd:PRK10263   453 QSTFAPQSTYQTEQTYQQPAAQEPLYQQPQP 483
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 88-180 1.34e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.37  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  88 DEEEVTYQSAPITQQ-----PAMQQTQKEVQIKPQKEMQVKPQKEVQVKPQKEM----QVKPQKEVQKEQPIQKEKPVEK 158
Cdd:TIGR02794  44 DPGAVAQQANRIQQQkkpaaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRaaaeKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100
                  ....*....|....*....|..
gi 1005571654 159 PSVIQKPpviEKQKPAEKENTK 180
Cdd:TIGR02794 124 AKAKQAA---EAKAKAEAEAER 142
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 92-180 2.73e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.21  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654  92 VTYQSAPITQQPAMQQTQKEVQIKPQKEMQVKP-QKEVQVKPQKEM-QVKPQKEVQKEQPIQKEKPVEKpsviQKPPVIE 169
Cdd:TIGR02794  41 VLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLeQQAEEAEKQRAAeQARQKELEQRAAAEKAAKQAEQ----AAKQAEE 116

                          90
                  ....*....|.
gi 1005571654 170 KQKPAEKENTK 180
Cdd:TIGR02794 117 KQKQAEEAKAK 127
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 56-174 3.05e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005571654   56 QQAGAGSAPPKQYVKEVQQKEFAATPTPLGIEDEEEVTYQSAPITQQPAMQQTQKEVQIKPQKEMQVKPQKEVQV---KP 132
Cdd:PRK10263   381 PQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTfapQS 460

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1005571654  133 QKEMQVKPQKEVQKEQPIQKEKPVEKPSVIQKPPVIEKQKPA 174
Cdd:PRK10263   461 TYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPA 502
 
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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