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Conserved domains on  [gi|1800525122|ref|WP_160378917|]
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type II secretion system protein GspC [Escherichia coli]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T2SSC super family cl44344
Type II secretion system protein C; This is the greater N-terminal region of GspC-type ...
 6-218 3.75e-95

Type II secretion system protein C; This is the greater N-terminal region of GspC-type proteins. GspC proteins form part of the sophisticated transport mechanism of Gram-negative pathogens for injecting divers proteins into their hosts, a type-II secretion system - T2SS. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interacts with the outer membrane secretin GspD via periplasmic domains, an interaction which is critical for the effectiveness of type II secretion.


The actual alignment was detected with superfamily member TIGR01713:

Pssm-ID: 457689 [Multi-domain]  Cd Length: 259  Bit Score: 279.02  E-value: 3.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122   6 KNGQIINQPTNAFQSDFSLAALWR--NENHAGVKDANPVAVNQETPKLSIALNGIVLTSNDETSFVLINEGSEQKRYSLN 83
Cdd:TIGR01713  34 VSKQISVNLANLQPSDLKLFELFGvfNEKSVSEVKTSPVSVNAPVSPLSLKLTGIVASSDRIRSIAIIEEGSEQVSLGIN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  84 EALESAPgTFIRKINKTSVVFETHGHYEKVTLHP-------------GLPDIIKQPDSESQNvLADYIIATPIRDGEQIY 150
Cdd:TIGR01713 114 ESFEGYK-AKIAKIEPDRVIFEYNGRYEPLELKNtkgeksnnsseivVSRRIIEELTKDPQK-MFDYIRLSPVMKNDKLE 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800525122 151 GLRLNPRKGLNAFTTSLLQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:TIGR01713 192 GYRLNPGKDPSLFYKSGLQDGDIAVALNGLDLRDPEQAFQALQMLREETNLTLTVERDGQREDIYVRF 259
 
Name Accession Description Interval E-value
typeII_sec_gspC TIGR01713
type II secretion system protein C; This model represents GspC, protein C of the main terminal ...
 6-218 3.75e-95

type II secretion system protein C; This model represents GspC, protein C of the main terminal branch of the general secretion pathway, also called type II secretion. This system transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273770 [Multi-domain]  Cd Length: 259  Bit Score: 279.02  E-value: 3.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122   6 KNGQIINQPTNAFQSDFSLAALWR--NENHAGVKDANPVAVNQETPKLSIALNGIVLTSNDETSFVLINEGSEQKRYSLN 83
Cdd:TIGR01713  34 VSKQISVNLANLQPSDLKLFELFGvfNEKSVSEVKTSPVSVNAPVSPLSLKLTGIVASSDRIRSIAIIEEGSEQVSLGIN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  84 EALESAPgTFIRKINKTSVVFETHGHYEKVTLHP-------------GLPDIIKQPDSESQNvLADYIIATPIRDGEQIY 150
Cdd:TIGR01713 114 ESFEGYK-AKIAKIEPDRVIFEYNGRYEPLELKNtkgeksnnsseivVSRRIIEELTKDPQK-MFDYIRLSPVMKNDKLE 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800525122 151 GLRLNPRKGLNAFTTSLLQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:TIGR01713 192 GYRLNPGKDPSLFYKSGLQDGDIAVALNGLDLRDPEQAFQALQMLREETNLTLTVERDGQREDIYVRF 259
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 42-218 3.09e-33

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 119.31  E-value: 3.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  42 VAVNQETPKLSIALNGIVLTSNDETSFVLI-NEGSEQKRYSLNEALEsaPGTFIRKINKTSVVFETHGHYEKVTLH---- 116
Cdd:COG3031    15 VLTDAPETRLNLTLLGVVASSDPERSFAIIaEGGGKQKSYRVGDEIP--GGATLVAVYRDRVILSNNGRLETLMLDgedy 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122 117 -------------PGLPDIIKQPDSESQ------------NVLADYIIATPIRDGEQIYGLRLNPRKGLNAFTTSLLQPG 171
Cdd:COG3031    93 aapaaaaaapassPAASSAAASAGGQEElevsrdellanpNELLDYIRLSPVREDGKLVGYRVNPGRPGSLFSKLGLQPG 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1800525122 172 DIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:COG3031   173 DVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQPVTLTYNL 219
PRK09681 PRK09681
putative type II secretion protein GspC; Provisional
 34-218 5.58e-08

putative type II secretion protein GspC; Provisional


Pssm-ID: 182027 [Multi-domain]  Cd Length: 276  Bit Score: 52.06  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  34 AGVKDANPVAVNQEtpKLSIALNGIVLTSNDEtsfVLINEGSEQKRYSLNEALESApGTFIRKINKTSVVFETHGHYEKV 113
Cdd:PRK09681   67 APVKQPEPAPVAET--RLNVVLRGIAFGARPG---AVIEEGGKQQVYLQGETLGSH-NAVIEEINRDHVMLRYQGKIERL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122 114 TL-------------------------HPG------LPDIIKQPDSESQNVLADYIIATPIRDgEQIYGLRLNPRKGLNA 162
Cdd:PRK09681  141 SLaeeerstvavtnkkavsdeakqavaEPAvsapveIPAAVRQALAKDPQKIFNYIQLTPVRK-EGIVGYAVKPGADRSL 219

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1800525122 163 FTTSLLQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:PRK09681  220 FDASGFKEGDIAIALNQQDFTDPRAMIALMRQLPSMDSIQLTVLRKGARHDISIAL 275
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 168-221 2.20e-03

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 36.53  E-value: 2.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1800525122 168 LQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSVGEL 221
Cdd:cd10838    51 LRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDRRQTLAVKPGDL 104
 
Name Accession Description Interval E-value
typeII_sec_gspC TIGR01713
type II secretion system protein C; This model represents GspC, protein C of the main terminal ...
 6-218 3.75e-95

type II secretion system protein C; This model represents GspC, protein C of the main terminal branch of the general secretion pathway, also called type II secretion. This system transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273770 [Multi-domain]  Cd Length: 259  Bit Score: 279.02  E-value: 3.75e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122   6 KNGQIINQPTNAFQSDFSLAALWR--NENHAGVKDANPVAVNQETPKLSIALNGIVLTSNDETSFVLINEGSEQKRYSLN 83
Cdd:TIGR01713  34 VSKQISVNLANLQPSDLKLFELFGvfNEKSVSEVKTSPVSVNAPVSPLSLKLTGIVASSDRIRSIAIIEEGSEQVSLGIN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  84 EALESAPgTFIRKINKTSVVFETHGHYEKVTLHP-------------GLPDIIKQPDSESQNvLADYIIATPIRDGEQIY 150
Cdd:TIGR01713 114 ESFEGYK-AKIAKIEPDRVIFEYNGRYEPLELKNtkgeksnnsseivVSRRIIEELTKDPQK-MFDYIRLSPVMKNDKLE 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1800525122 151 GLRLNPRKGLNAFTTSLLQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:TIGR01713 192 GYRLNPGKDPSLFYKSGLQDGDIAVALNGLDLRDPEQAFQALQMLREETNLTLTVERDGQREDIYVRF 259
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 42-218 3.09e-33

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 119.31  E-value: 3.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  42 VAVNQETPKLSIALNGIVLTSNDETSFVLI-NEGSEQKRYSLNEALEsaPGTFIRKINKTSVVFETHGHYEKVTLH---- 116
Cdd:COG3031    15 VLTDAPETRLNLTLLGVVASSDPERSFAIIaEGGGKQKSYRVGDEIP--GGATLVAVYRDRVILSNNGRLETLMLDgedy 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122 117 -------------PGLPDIIKQPDSESQ------------NVLADYIIATPIRDGEQIYGLRLNPRKGLNAFTTSLLQPG 171
Cdd:COG3031    93 aapaaaaaapassPAASSAAASAGGQEElevsrdellanpNELLDYIRLSPVREDGKLVGYRVNPGRPGSLFSKLGLQPG 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1800525122 172 DIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:COG3031   173 DVITSINGQDLTDPAQALELLQQLRDASEVTLTVERNGQPVTLTYNL 219
PRK09681 PRK09681
putative type II secretion protein GspC; Provisional
 34-218 5.58e-08

putative type II secretion protein GspC; Provisional


Pssm-ID: 182027 [Multi-domain]  Cd Length: 276  Bit Score: 52.06  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122  34 AGVKDANPVAVNQEtpKLSIALNGIVLTSNDEtsfVLINEGSEQKRYSLNEALESApGTFIRKINKTSVVFETHGHYEKV 113
Cdd:PRK09681   67 APVKQPEPAPVAET--RLNVVLRGIAFGARPG---AVIEEGGKQQVYLQGETLGSH-NAVIEEINRDHVMLRYQGKIERL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1800525122 114 TL-------------------------HPG------LPDIIKQPDSESQNVLADYIIATPIRDgEQIYGLRLNPRKGLNA 162
Cdd:PRK09681  141 SLaeeerstvavtnkkavsdeakqavaEPAvsapveIPAAVRQALAKDPQKIFNYIQLTPVRK-EGIVGYAVKPGADRSL 219

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1800525122 163 FTTSLLQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSV 218
Cdd:PRK09681  220 FDASGFKEGDIAIALNQQDFTDPRAMIALMRQLPSMDSIQLTVLRKGARHDISIAL 275
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 168-221 8.08e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 39.90  E-value: 8.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1800525122 168 LQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSVGEL 221
Cdd:TIGR02037 275 LKAGDVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILRKGKEKTITVTLGAS 328
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 168-221 2.20e-03

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 36.53  E-value: 2.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1800525122 168 LQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSVGEL 221
Cdd:cd10838    51 LRRGDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLRGDRRQTLAVKPGDL 104
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 168-221 3.51e-03

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 37.82  E-value: 3.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1800525122 168 LQPGDIALRINNLSLTHPDEVSQALSLLLTQQSAQFTIRRNGVPRLINVSVGEL 221
Cdd:COG0265   219 LRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTLGER 272
 
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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