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Conserved domains on  [gi|499658028|ref|WP_011338762|]
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OmpA family protein [Cereibacter sphaeroides]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 182-337 7.27e-25

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd13566:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 245  Bit Score: 103.05  E-value: 7.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 182 VLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKELGGPDMPLVLHALA-----RDISLEAALEArlGRPIAAEITH 256
Cdd:cd13566   79 VIAYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDegsgtRDYFEELVLGK--GEFIRNAVVA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 257 PDLASLAAAVARDPYALAITG-QTARGAARVLPLTDSCGfplVPSPLAVKSEDYPLALPVFLVSPPRRLPLfAREFLEFL 335
Cdd:cd13566  157 PSNGALVQAVAGDPNAIGYVGlGYVDENKKVKALKVDGV---APTVENIKSGKYPLSRPLFLYTKGEPSPA-VKAFIDFA 232


                 ..
gi 499658028 336 SS 337
Cdd:cd13566  233 LS 234
OmpA_C-like super family cl30079
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 396-503 7.46e-13

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


The actual alignment was detected with superfamily member cd07185:

Pssm-ID: 453091 [Multi-domain]  Cd Length: 106  Bit Score: 64.88  E-value: 7.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 396 SITFRFEEGTDSLEPQSRESLSELIKLLEigRFRGQQLMLVGFSDGRGPARGNLDLSreraeavaaalreavpE------ 469
Cdd:cd07185    1 LITIYFDFGSAELTPEAKPLLDKLAEVLK--KNPDAKIRIEGHTDSRGSDAYNQELS----------------Erraeav 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499658028 470 ------LGPP----LVEGFGEALPLACDTTVAGRRMNRRVELWL 503
Cdd:cd07185   63 adylvsKGVDasriTAVGYGESRPIASNDTEEGRAKNRRVEIVI 106
 
Name Accession Description Interval E-value
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 182-337 7.27e-25

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270284 [Multi-domain]  Cd Length: 245  Bit Score: 103.05  E-value: 7.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 182 VLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKELGGPDMPLVLHALA-----RDISLEAALEArlGRPIAAEITH 256
Cdd:cd13566   79 VIAYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDegsgtRDYFEELVLGK--GEFIRNAVVA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 257 PDLASLAAAVARDPYALAITG-QTARGAARVLPLTDSCGfplVPSPLAVKSEDYPLALPVFLVSPPRRLPLfAREFLEFL 335
Cdd:cd13566  157 PSNGALVQAVAGDPNAIGYVGlGYVDENKKVKALKVDGV---APTVENIKSGKYPLSRPLFLYTKGEPSPA-VKAFIDFA 232


                 ..
gi 499658028 336 SS 337
Cdd:cd13566  233 LS 234
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 171-350 4.87e-22

ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 95.72  E-value: 4.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 171 AAHADPGMTTRVLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKELGG--PDMPLVLHALA-----RDISLEAALE 243
Cdd:COG0226   70 AKENGVELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGklPDEPITVVGRSdgsgtTDYFTEYLLG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 244 ArlGRPIAAEIT-HPDLASLAAAVARDPYALAITG--QTARGAARVLPLTDSCGFPLVPSPLAVKSEDYPLALPVFLV-- 318
Cdd:COG0226  150 V--GAEVREGVEgAEGNEGVVQAVAQTPGAIGYVGlsYAEQNKLKALAIDNKAGKFVEPTAENIAAGSYPLSRPLYIYvk 227

                        170       180       190
                 ....*....|....*....|....*....|...
gi 499658028 319 -SPPRRLPLfAREFLEFLSSAPAQAAVAEAGFV 350
Cdd:COG0226  228 kEPDAKAPA-VKAFLDFVLSDGGQKIVEKLGYV 259
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 396-503 7.46e-13

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 64.88  E-value: 7.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 396 SITFRFEEGTDSLEPQSRESLSELIKLLEigRFRGQQLMLVGFSDGRGPARGNLDLSreraeavaaalreavpE------ 469
Cdd:cd07185    1 LITIYFDFGSAELTPEAKPLLDKLAEVLK--KNPDAKIRIEGHTDSRGSDAYNQELS----------------Erraeav 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499658028 470 ------LGPP----LVEGFGEALPLACDTTVAGRRMNRRVELWL 503
Cdd:cd07185   63 adylvsKGVDasriTAVGYGESRPIASNDTEEGRAKNRRVEIVI 106
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 170-337 3.00e-09

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 57.94  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  170 IAAHADPGMTTRVLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKElGGPDMPLVL---------------HALAR 234
Cdd:pfam12849  76 FGANGAGGLVEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFvsrgdnsgttelfstHLKEK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  235 DISLEAALEARLGRPIAAEITHP---DLASLAAAVARDPYALA----ITGQTARGAARVLPLTDSCGfPLVPSPLAVKSE 307
Cdd:pfam12849 155 GPWGAAGIGAAGSPGVASVVAGPgaiGYVEVSYALANLGYTLAdvagGTYLSFAKALKVAKINPGAG-LVIPLEEAIADG 233

                         170       180       190
                  ....*....|....*....|....*....|..
gi 499658028  308 DYPLALPVFLVSPPRRLPLF--AREFLEFLSS 337
Cdd:pfam12849 234 DYPLSRPYYVIVKNPPKGPAplAKAFLDFLLS 265
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 182-350 2.98e-07

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 52.06  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  182 VLALDALVPIVAADN-PVPRVSTPDLARALSGEISNWKELGG--PDMPLVLHALARDISLEAALEARL---GRPIAAEIT 255
Cdd:TIGR02136 113 KVAVDGLAVVVNKKNvPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKPIVVVGRNAGSGTRDTFEEEVmgkAKIKPGKNE 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  256 HPDLASLAAAVARDPYALAITGQTARgAARVLPLTDScgfPLVPSPLAVKSEDYPLALPVFLV--SPPRRLPLfAREFLE 333
Cdd:TIGR02136 193 QESNGAVVSIVSSNPGAIGYLGLGYV-DDSVKTLKVN---GVEPSKENIANGSYPLSRPLFMYvnGKPKKPEL-VAEFID 267

                         170
                  ....*....|....*...
gi 499658028  334 F-LSSAPAQAAVAEAGFV 350
Cdd:TIGR02136 268 FvLSDDGGERIVEELGYV 285
motB PRK07734
flagellar motor protein MotB; Reviewed
 468-508 4.90e-04

flagellar motor protein MotB; Reviewed


Pssm-ID: 236080 [Multi-domain]  Cd Length: 259  Bit Score: 42.04  E-value: 4.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499658028 468 PELGPPL--VEGFGEALPLACDTTVAGRRMNRRVELWLRPLTD 508
Cdd:PRK07734 214 KELDPEKfsAKGYGEYKPIASNDTAEGRAKNRRVEVLILPLTE 256
MotB COG1360
Flagellar motor protein MotB [Cell motility];
393-505 6.08e-04

Flagellar motor protein MotB [Cell motility];


Pssm-ID: 440971 [Multi-domain]  Cd Length: 174  Bit Score: 40.60  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 393 DRLSITFR----FEEGTDSLEPQSRESLSELIKLLeigRFRGQQLMLVGFSD----GRGPARGNLDLSRERAEAVAAALR 464
Cdd:COG1360   51 EGLVIEIQdrvlFDSGSAELTPEGRELLDKIAAVL---AEVPNRIRVEGHTDnvpiSTARFPSNWELSAARAAAVVRYLI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499658028 465 eavpELG-PP---LVEGFGEALPLACDTTVAGRRMNRRVELWLRP 505
Cdd:COG1360  128 ----EGGvPPerlSAVGYGDTRPLAPNDTPEGRARNRRVEIVILR 168
OmpA pfam00691
OmpA family; The Pfam entry also includes MotB and related proteins which are not included in ...
 401-455 9.02e-04

OmpA family; The Pfam entry also includes MotB and related proteins which are not included in the Prosite family.


Pssm-ID: 425825 [Multi-domain]  Cd Length: 95  Bit Score: 38.50  E-value: 9.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499658028  401 FEEGTDSLEPQSRESLSELIKLLEIGRFRGQqLMLVGFSDGRGPARGNLDLSRER 455
Cdd:pfam00691   1 FDPGSSQLTPKAKATLDEIADLLKFPELKNT-ITIEGHTDTVGSAAYNWELSQRR 54
type_VI_ompA TIGR03350
type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, ...
 392-500 2.58e-03

type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, the Gram-negative bacterial outer membrane protein OmpA (with an N-terminal outer membrane beta barrel domain) share a C-terminal peptidoglycan-associating homology region. This model describes a domain found fused to type VI secretion system homologs of the type IV system protein DotU (see model TIGR03349), with OmpA/MotB homology. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274533 [Multi-domain]  Cd Length: 137  Bit Score: 38.44  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  392 ADRLSITFR----FEEGTDSLEPQSRESLSELIKLLEIGRFRgqqLMLVGFSDGRgPAR-----GNLDLSRERAEAVAAA 462
Cdd:TIGR03350  21 GDRSVVRLRgdelFASGSAEVRAEFEPLLLRIAKALAAVPGR---ITVVGHTDNV-PIRtarfpSNWHLSEARAKAVADV 96

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499658028  463 LREAVPELGPPLVEGFGEALPLACDTTVAGRRMNRRVE 500
Cdd:TIGR03350  97 LAQAGGPAGRVRAEGRGDSEPIASNATAAGRARNRRVE 134
 
Name Accession Description Interval E-value
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 182-337 7.27e-25

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270284 [Multi-domain]  Cd Length: 245  Bit Score: 103.05  E-value: 7.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 182 VLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKELGGPDMPLVLHALA-----RDISLEAALEArlGRPIAAEITH 256
Cdd:cd13566   79 VIAYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDegsgtRDYFEELVLGK--GEFIRNAVVA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 257 PDLASLAAAVARDPYALAITG-QTARGAARVLPLTDSCGfplVPSPLAVKSEDYPLALPVFLVSPPRRLPLfAREFLEFL 335
Cdd:cd13566  157 PSNGALVQAVAGDPNAIGYVGlGYVDENKKVKALKVDGV---APTVENIKSGKYPLSRPLFLYTKGEPSPA-VKAFIDFA 232


                 ..
gi 499658028 336 SS 337
Cdd:cd13566  233 LS 234
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 169-337 2.13e-24

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 101.49  E-value: 2.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 169 VIAAHADPGMTTR----------------VLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKELGGPDMPLVLHal 232
Cdd:cd13653   46 LIEGTADIGMASRplkaeekaaasglvehVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVI-- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 233 ARDI---SLEAALEARLGR--PIAAEITHPDLASLAAAVARDPYALAITGQTARGAARVLPLTDSCGfplVPSPLAVKSE 307
Cdd:cd13653  124 SREEgsgTRETFEELVLGKkdFAKNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVDDSKVKALSVDGV---APTPENIKSG 200

                        170       180       190
                 ....*....|....*....|....*....|..
gi 499658028 308 DYPLALPVFLV--SPPRRLplfAREFLEFLSS 337
Cdd:cd13653  201 KYPLSRPLYLYtkGEPSGL---VKAFIDFALS 229
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 171-350 4.87e-22

ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 95.72  E-value: 4.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 171 AAHADPGMTTRVLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKELGG--PDMPLVLHALA-----RDISLEAALE 243
Cdd:COG0226   70 AKENGVELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGklPDEPITVVGRSdgsgtTDYFTEYLLG 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 244 ArlGRPIAAEIT-HPDLASLAAAVARDPYALAITG--QTARGAARVLPLTDSCGFPLVPSPLAVKSEDYPLALPVFLV-- 318
Cdd:COG0226  150 V--GAEVREGVEgAEGNEGVVQAVAQTPGAIGYVGlsYAEQNKLKALAIDNKAGKFVEPTAENIAAGSYPLSRPLYIYvk 227

                        170       180       190
                 ....*....|....*....|....*....|...
gi 499658028 319 -SPPRRLPLfAREFLEFLSSAPAQAAVAEAGFV 350
Cdd:COG0226  228 kEPDAKAPA-VKAFLDFVLSDGGQKIVEKLGYV 259
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 396-503 7.46e-13

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 64.88  E-value: 7.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 396 SITFRFEEGTDSLEPQSRESLSELIKLLEigRFRGQQLMLVGFSDGRGPARGNLDLSreraeavaaalreavpE------ 469
Cdd:cd07185    1 LITIYFDFGSAELTPEAKPLLDKLAEVLK--KNPDAKIRIEGHTDSRGSDAYNQELS----------------Erraeav 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499658028 470 ------LGPP----LVEGFGEALPLACDTTVAGRRMNRRVELWL 503
Cdd:cd07185   63 adylvsKGVDasriTAVGYGESRPIASNDTEEGRAKNRRVEIVI 106
OmpA COG2885
Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall ...
 231-505 1.26e-10

Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442131 [Multi-domain]  Cd Length: 294  Bit Score: 62.49  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 231 ALARDISLEAALEARLGRPIAAEITHPDLASLAAAVARDPYALAITGQTARGAARVLPLTDSCGFPLVPSPLAVKSEDYP 310
Cdd:COG2885   20 LSGAALLLALLGVLGSAGGLLSLADDLAEASAGAAGGAAAGAEAGGLSAGLELLDAGSLSATAAAGAAALLVLLAALGAL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 311 LALPVFLVSPPRRLPLFAREFLEFLSSAPAQAAVAEAGFVDRRPSQVPLASDGQRLMNAIRIAGEEVPLDEVKRLTDLMA 390
Cdd:COG2885  100 GAGLAALLLAIAAAASAAAADALALAAGAAAALGALGASAAAAAAALAAAKALGDSAAAALDAAAKAEAAAAAAALLPAA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 391 GADR-LSITFRFEEGTDSLEPQSRESLSELIKLLEigRFRGQQLMLVGFSDGRGPARGNLDLSR----------Eraeav 459
Cdd:COG2885  180 VAEVvLLSNVYFDFDSAELTPEAKAALDELAALLK--ENPDLRIEIEGHTDSRGSDAYNLALSErraeavkdylV----- 252

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 499658028 460 aaalreavpELGPP----LVEGFGEALPLACDTTVAGRRMNRRVELWLRP 505
Cdd:COG2885  253 ---------SKGIPasriTAVGYGESRPVASNDTEEGRAKNRRVEIVVLK 293
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 170-337 3.00e-09

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 57.94  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  170 IAAHADPGMTTRVLALDALVPIVAADNPVPRVSTPDLARALSGEISNWKElGGPDMPLVL---------------HALAR 234
Cdd:pfam12849  76 FGANGAGGLVEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFvsrgdnsgttelfstHLKEK 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  235 DISLEAALEARLGRPIAAEITHP---DLASLAAAVARDPYALA----ITGQTARGAARVLPLTDSCGfPLVPSPLAVKSE 307
Cdd:pfam12849 155 GPWGAAGIGAAGSPGVASVVAGPgaiGYVEVSYALANLGYTLAdvagGTYLSFAKALKVAKINPGAG-LVIPLEEAIADG 233

                         170       180       190
                  ....*....|....*....|....*....|..
gi 499658028  308 DYPLALPVFLVSPPRRLPLF--AREFLEFLSS 337
Cdd:pfam12849 234 DYPLSRPYYVIVKNPPKGPAplAKAFLDFLLS 265
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 182-350 2.98e-07

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 52.06  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  182 VLALDALVPIVAADN-PVPRVSTPDLARALSGEISNWKELGG--PDMPLVLHALARDISLEAALEARL---GRPIAAEIT 255
Cdd:TIGR02136 113 KVAVDGLAVVVNKKNvPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKPIVVVGRNAGSGTRDTFEEEVmgkAKIKPGKNE 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  256 HPDLASLAAAVARDPYALAITGQTARgAARVLPLTDScgfPLVPSPLAVKSEDYPLALPVFLV--SPPRRLPLfAREFLE 333
Cdd:TIGR02136 193 QESNGAVVSIVSSNPGAIGYLGLGYV-DDSVKTLKVN---GVEPSKENIANGSYPLSRPLFMYvnGKPKKPEL-VAEFID 267

                         170
                  ....*....|....*...
gi 499658028  334 F-LSSAPAQAAVAEAGFV 350
Cdd:TIGR02136 268 FvLSDDGGERIVEELGYV 285
motB PRK07734
flagellar motor protein MotB; Reviewed
 468-508 4.90e-04

flagellar motor protein MotB; Reviewed


Pssm-ID: 236080 [Multi-domain]  Cd Length: 259  Bit Score: 42.04  E-value: 4.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 499658028 468 PELGPPL--VEGFGEALPLACDTTVAGRRMNRRVELWLRPLTD 508
Cdd:PRK07734 214 KELDPEKfsAKGYGEYKPIASNDTAEGRAKNRRVEVLILPLTE 256
MotB COG1360
Flagellar motor protein MotB [Cell motility];
393-505 6.08e-04

Flagellar motor protein MotB [Cell motility];


Pssm-ID: 440971 [Multi-domain]  Cd Length: 174  Bit Score: 40.60  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 393 DRLSITFR----FEEGTDSLEPQSRESLSELIKLLeigRFRGQQLMLVGFSD----GRGPARGNLDLSRERAEAVAAALR 464
Cdd:COG1360   51 EGLVIEIQdrvlFDSGSAELTPEGRELLDKIAAVL---AEVPNRIRVEGHTDnvpiSTARFPSNWELSAARAAAVVRYLI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499658028 465 eavpELG-PP---LVEGFGEALPLACDTTVAGRRMNRRVELWLRP 505
Cdd:COG1360  128 ----EGGvPPerlSAVGYGDTRPLAPNDTPEGRARNRRVEIVILR 168
OmpA pfam00691
OmpA family; The Pfam entry also includes MotB and related proteins which are not included in ...
 401-455 9.02e-04

OmpA family; The Pfam entry also includes MotB and related proteins which are not included in the Prosite family.


Pssm-ID: 425825 [Multi-domain]  Cd Length: 95  Bit Score: 38.50  E-value: 9.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499658028  401 FEEGTDSLEPQSRESLSELIKLLEIGRFRGQqLMLVGFSDGRGPARGNLDLSRER 455
Cdd:pfam00691   1 FDPGSSQLTPKAKATLDEIADLLKFPELKNT-ITIEGHTDTVGSAAYNWELSQRR 54
type_VI_ompA TIGR03350
type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, ...
 392-500 2.58e-03

type VI secretion system peptidoglycan-associated domain; The flagellar motor protein MotB, the Gram-negative bacterial outer membrane protein OmpA (with an N-terminal outer membrane beta barrel domain) share a C-terminal peptidoglycan-associating homology region. This model describes a domain found fused to type VI secretion system homologs of the type IV system protein DotU (see model TIGR03349), with OmpA/MotB homology. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274533 [Multi-domain]  Cd Length: 137  Bit Score: 38.44  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028  392 ADRLSITFR----FEEGTDSLEPQSRESLSELIKLLEIGRFRgqqLMLVGFSDGRgPAR-----GNLDLSRERAEAVAAA 462
Cdd:TIGR03350  21 GDRSVVRLRgdelFASGSAEVRAEFEPLLLRIAKALAAVPGR---ITVVGHTDNV-PIRtarfpSNWHLSEARAKAVADV 96

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499658028  463 LREAVPELGPPLVEGFGEALPLACDTTVAGRRMNRRVE 500
Cdd:TIGR03350  97 LAQAGGPAGRVRAEGRGDSEPIASNATAAGRARNRRVE 134
PRK10510 PRK10510
OmpA family lipoprotein;
401-506 8.41e-03

OmpA family lipoprotein;


Pssm-ID: 182507 [Multi-domain]  Cd Length: 219  Bit Score: 37.93  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499658028 401 FEEGTDSLEPQSRESLSELIKLLeiGRFRGQQLMLVGFSDGRGPARGNLDLSRERAEAVAAALREAVPELGPPLVEGFGE 480
Cdd:PRK10510 116 FDSSSATLKPAGANTLTGVAMVL--KEYPKTAVNVVGYTDSTGSHDLNMRLSQQRADSVASALITQGVDASRIRTQGMGP 193

                         90       100
                 ....*....|....*....|....*.
gi 499658028 481 ALPLACDTTVAGRRMNRRVELWLRPL 506
Cdd:PRK10510 194 ANPIASNSTAEGKAQNRRVEITLSPL 219
 
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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