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Conserved domains on  [gi|502825945|ref|WP_013060921|]
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SusD/RagB family nutrient-binding outer membrane lipoprotein [Salinibacter ruber]

Protein Classification

RagB/SusD family nutrient uptake outer membrane protein( domain architecture ID 716162)

RagB/SusD family nutrient uptake outer membrane protein similar to Bacteroides thetaiotaomicron starch-binding protein SusD, which is a major starch-binding protein present at the surface of the cell and mediates starch-binding before starch transport in the periplasm for degradation

CATH:  1.20.120.840
Gene Ontology:  GO:0009279|GO:0016020|GO:2001070
PubMed:  18611370
SCOP:  4001583

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
SusD-like_2 super family cl26038
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with ...
70-498 1.08e-79

Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.


The actual alignment was detected with superfamily member pfam12771:

Pssm-ID: 463695  Cd Length: 415  Bit Score: 255.79  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945   70 TNLIYTMPIvqHIANPgfYAGNFNQYVGAWSASFFD--TRYGGGPNGSNF---------LRTVTNAETLISELEGKPRQV 138
Cdd:pfam12771  14 TNALYNLAN--NNTNE--NYNINRLLMQYWTPTTYGdeSRYDFTRNIGNSfwngyyrwvLKNLKEMKNLAKEEAIDNANN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  139 NRLAATRIMRVLTFQRLTDVYGDVPYFDAGKGalEGEFTPHYTRQDSIYMDLHDELRAAVDQFDASqPTFGGADLFFNGS 218
Cdd:pfam12771  90 NYIAVALILKAYVYSNLTDTFGDVPYSEALRG--EEGLQPKYDSQEDIYKDLLADLDEANALYDTG-MGYNAGDILYNGD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  219 IEQWKRFANSLQLRLALRVVKVRPDLAQSWAEEAVNADGGVMQSVEDDAYVPHQ-SGPsggpagfNTNAHSEVMQSFPGQ 297
Cdd:pfam12771 167 VEKWKKFANSLRLRMLLRISKVDPAKAKTEFESAIAAGYPVFESNADNALLPYTgSTP-------NENPWYNLLVTRAQD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  298 W-LSETFVDWMKDKSDPRLTEYgaLAPGGLDSALVedpaqqrGMPNGFDNNelaasneytDDLDQYTRIHPNLRDRNDPM 376
Cdd:pfam12771 240 FaMSAFFVDELNGLNDPRLPVF--FTPNNIIGEYV-------GVPYGYVGD---------NSYFDYSTSGDNVIQVTAPM 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  377 FFQTYAEVELMLAEAAVRGWNVPGSAEAHYEAGVRAAMNYITrygentsvSDSEITQYLSDNSLPSGREARLRAINNQYW 456
Cdd:pfam12771 302 VLLTYSEVEFILAEAAQRGWNISGTAAEHYNKGIKASIEQWG--------GAADPAAYLAQPAVAYNTATGLEKIGLQKW 373
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 502825945  457 AATFLNGIESWSNWRRSGYPELTPAPEEGDTGGQFIRRLDYP 498
Cdd:pfam12771 374 LALYFRGYEAWFEWRRTGFPKLPPTGDGELNNGVIPVRLLYP 415
 
Name Accession Description Interval E-value
SusD-like_2 pfam12771
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with ...
70-498 1.08e-79

Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.


Pssm-ID: 463695  Cd Length: 415  Bit Score: 255.79  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945   70 TNLIYTMPIvqHIANPgfYAGNFNQYVGAWSASFFD--TRYGGGPNGSNF---------LRTVTNAETLISELEGKPRQV 138
Cdd:pfam12771  14 TNALYNLAN--NNTNE--NYNINRLLMQYWTPTTYGdeSRYDFTRNIGNSfwngyyrwvLKNLKEMKNLAKEEAIDNANN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  139 NRLAATRIMRVLTFQRLTDVYGDVPYFDAGKGalEGEFTPHYTRQDSIYMDLHDELRAAVDQFDASqPTFGGADLFFNGS 218
Cdd:pfam12771  90 NYIAVALILKAYVYSNLTDTFGDVPYSEALRG--EEGLQPKYDSQEDIYKDLLADLDEANALYDTG-MGYNAGDILYNGD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  219 IEQWKRFANSLQLRLALRVVKVRPDLAQSWAEEAVNADGGVMQSVEDDAYVPHQ-SGPsggpagfNTNAHSEVMQSFPGQ 297
Cdd:pfam12771 167 VEKWKKFANSLRLRMLLRISKVDPAKAKTEFESAIAAGYPVFESNADNALLPYTgSTP-------NENPWYNLLVTRAQD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  298 W-LSETFVDWMKDKSDPRLTEYgaLAPGGLDSALVedpaqqrGMPNGFDNNelaasneytDDLDQYTRIHPNLRDRNDPM 376
Cdd:pfam12771 240 FaMSAFFVDELNGLNDPRLPVF--FTPNNIIGEYV-------GVPYGYVGD---------NSYFDYSTSGDNVIQVTAPM 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  377 FFQTYAEVELMLAEAAVRGWNVPGSAEAHYEAGVRAAMNYITrygentsvSDSEITQYLSDNSLPSGREARLRAINNQYW 456
Cdd:pfam12771 302 VLLTYSEVEFILAEAAQRGWNISGTAAEHYNKGIKASIEQWG--------GAADPAAYLAQPAVAYNTATGLEKIGLQKW 373
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 502825945  457 AATFLNGIESWSNWRRSGYPELTPAPEEGDTGGQFIRRLDYP 498
Cdd:pfam12771 374 LALYFRGYEAWFEWRRTGFPKLPPTGDGELNNGVIPVRLLYP 415
SusD cd08977
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
102-474 4.70e-11

starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.


Pssm-ID: 185760 [Multi-domain]  Cd Length: 359  Bit Score: 64.36  E-value: 4.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 102 SFFDTRYGGGPNGSNFLRTVTNAETLISELEGKPR----QVNR-LAATRIMRVLTFQRLTDVYGDVPYFDAGKgalEGEF 176
Cdd:cd08977   54 NNPNDSAFGTSSWNGVYTNINNANIFLEKIDEASElteaNRNRyKGEAKFIRALAYFYLTRLFGGVPLSTAAD---QGTE 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 177 TPHYTRQDSIYMDLHDELRAAVDQFdasqPTFGGADLFF--NGSIEQWKRFANSLQLRLALRVVKVRPDLAQSWAEEAVN 254
Cdd:cd08977  131 TPPRDSQEEVYTQILADLDEAIALL----PEASSAQDFYiyFGDGRAWKKAARALLARVYLYLANYTAADYAEALTAAEK 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 255 ADGGVMQSVEDDAYVPH-------------QSGPSGGPAGFNTNAhsevmQSFPGQWLSETFVDWMKDKSDPRlteygal 321
Cdd:cd08977  207 SFKGGVTLLTNLFGENAanskedifeiyyaDSGDNSNPLGSLNNN-----NGYANFRVSADIIDKLDGYGDPR------- 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 322 apggldsalvedpaqqrgmpngfdnneLAASNEYtddldqytrihpnlrdrndpmfFQTYAEVELMLAEAAVRGWNVpGS 401
Cdd:cd08977  275 ---------------------------LSLAPIP----------------------IIRYAEVLLLRAEALARLGNG-AD 304
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825945 402 AEAHYEAGVRAAmnyitrYGENTSVSDSEITQylsdnslpsgrEARLRAINNQYWAATFLNGIeSWSNWRRSG 474
Cdd:cd08977  305 AIEYLNAVRRRS------GGNAANNTSQASTA-----------EELLEEILDERRLELFGEGH-RWYDLRRTG 359
 
Name Accession Description Interval E-value
SusD-like_2 pfam12771
Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with ...
70-498 1.08e-79

Starch-binding associating with outer membrane; SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.


Pssm-ID: 463695  Cd Length: 415  Bit Score: 255.79  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945   70 TNLIYTMPIvqHIANPgfYAGNFNQYVGAWSASFFD--TRYGGGPNGSNF---------LRTVTNAETLISELEGKPRQV 138
Cdd:pfam12771  14 TNALYNLAN--NNTNE--NYNINRLLMQYWTPTTYGdeSRYDFTRNIGNSfwngyyrwvLKNLKEMKNLAKEEAIDNANN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  139 NRLAATRIMRVLTFQRLTDVYGDVPYFDAGKGalEGEFTPHYTRQDSIYMDLHDELRAAVDQFDASqPTFGGADLFFNGS 218
Cdd:pfam12771  90 NYIAVALILKAYVYSNLTDTFGDVPYSEALRG--EEGLQPKYDSQEDIYKDLLADLDEANALYDTG-MGYNAGDILYNGD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  219 IEQWKRFANSLQLRLALRVVKVRPDLAQSWAEEAVNADGGVMQSVEDDAYVPHQ-SGPsggpagfNTNAHSEVMQSFPGQ 297
Cdd:pfam12771 167 VEKWKKFANSLRLRMLLRISKVDPAKAKTEFESAIAAGYPVFESNADNALLPYTgSTP-------NENPWYNLLVTRAQD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  298 W-LSETFVDWMKDKSDPRLTEYgaLAPGGLDSALVedpaqqrGMPNGFDNNelaasneytDDLDQYTRIHPNLRDRNDPM 376
Cdd:pfam12771 240 FaMSAFFVDELNGLNDPRLPVF--FTPNNIIGEYV-------GVPYGYVGD---------NSYFDYSTSGDNVIQVTAPM 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  377 FFQTYAEVELMLAEAAVRGWNVPGSAEAHYEAGVRAAMNYITrygentsvSDSEITQYLSDNSLPSGREARLRAINNQYW 456
Cdd:pfam12771 302 VLLTYSEVEFILAEAAQRGWNISGTAAEHYNKGIKASIEQWG--------GAADPAAYLAQPAVAYNTATGLEKIGLQKW 373
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 502825945  457 AATFLNGIESWSNWRRSGYPELTPAPEEGDTGGQFIRRLDYP 498
Cdd:pfam12771 374 LALYFRGYEAWFEWRRTGFPKLPPTGDGELNNGVIPVRLLYP 415
SusD-like pfam12741
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member ...
146-531 9.50e-65

Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member of which, BT1043, is an outer membrane lipoprotein involved in host glycan metabolism. The structures of this and SusD-homologs in the family are dominated by tetratrico peptide repeats that may facilitate association with outer membrane beta-barrel transporters required for glycan uptake. The structure of BT1043 complexed with N-acetyllactosamine reveals that recognition is mediated via hydrogen bonding interactions with the reducing end of beta-N-acetylglucosamine, suggesting a role in binding glycans liberated from the mucin polypeptide. Mammalian distal gut bacteria have an expanded capacity to utilize glycans. In the absence of dietary sources, some species rely on host-derived mucosal glycans. The ability of Bacteroides thetaiotaomicron, a prominent human gut symbiont, to forage host glycans contributes to both its ability to persist within an individual host and its ability to be transmitted naturally to new hosts at birth.


Pssm-ID: 432756  Cd Length: 495  Bit Score: 218.68  E-value: 9.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  146 IMRVLTFQRLTDVYGDVPYFDAGKGALegefTPHYTRQDSIYMDLHDELRAAVDQFD----ASQPTFGGADLFFNGSIEQ 221
Cdd:pfam12741 114 ILKVAAMHRVTDIYGPIPYSKAGSGKL----TVPYDSQEDVYKQFFKELDEAIAVLTpyrtAGFSSFPDYDLVYGGDVEK 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  222 WKRFANSLQLRLALRVVKVRPDLAQSWAEEAVNADGGVMQSVEDDAYVphQSGPSGGPagFNTNAHSevmqsfpgqW--- 298
Cdd:pfam12741 190 WVKFANSLKLRLAMRISYVDPALAKQYAEKAVNHEIGVIETNDDNAKI--SSLTYKNP--LYTIANS---------Ygdt 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  299 -LSETFVDWMKDKSDPRLTEYgalapggLDSALVEDPAQQRGMPNGfdNNELAASNEYtddlDQYTRIHPNlrdRNDPMF 377
Cdd:pfam12741 257 rMGADIESYLNGYNDPRLEKY-------FTKSTFPDGGGYKGIRAG--INIPSDKGAY----RKYSKPNVT---ETTPLY 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  378 FQTYAEVELMLAEAAVRGWNVPGSAEAHYEAGVR---------AAMNYITrygENTSVS---DSEITQYLSDNSLPS--- 442
Cdd:pfam12741 321 WMTAAEVAFLRAEGALRGWNMGGTAKDLYEEGVTlsfeqwgvsGADAYLA---DSTSKPadyTDPLGPYYSAAGAPStit 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945  443 -------GREARLRAINNQYWAATFLNGIESWSNWRRSGYPELTPAPEEGDTG----GQFIRRLDYPQGERDLNGDNYQE 511
Cdd:pfam12741 398 ikwddaaTNEEKLERIITQKWIALFPNGQEAWSEFRRTGYPKLFPVADNKSGGvidtERGIRRLPYPESEYTNNKANYNK 477
                         410       420
                  ....*....|....*....|
gi 502825945  512 AreRQNITQSNRLTARVWWD 531
Cdd:pfam12741 478 A--VSLLGGPDNGGTRLWWD 495
SusD cd08977
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
102-474 4.70e-11

starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.


Pssm-ID: 185760 [Multi-domain]  Cd Length: 359  Bit Score: 64.36  E-value: 4.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 102 SFFDTRYGGGPNGSNFLRTVTNAETLISELEGKPR----QVNR-LAATRIMRVLTFQRLTDVYGDVPYFDAGKgalEGEF 176
Cdd:cd08977   54 NNPNDSAFGTSSWNGVYTNINNANIFLEKIDEASElteaNRNRyKGEAKFIRALAYFYLTRLFGGVPLSTAAD---QGTE 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 177 TPHYTRQDSIYMDLHDELRAAVDQFdasqPTFGGADLFF--NGSIEQWKRFANSLQLRLALRVVKVRPDLAQSWAEEAVN 254
Cdd:cd08977  131 TPPRDSQEEVYTQILADLDEAIALL----PEASSAQDFYiyFGDGRAWKKAARALLARVYLYLANYTAADYAEALTAAEK 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 255 ADGGVMQSVEDDAYVPH-------------QSGPSGGPAGFNTNAhsevmQSFPGQWLSETFVDWMKDKSDPRlteygal 321
Cdd:cd08977  207 SFKGGVTLLTNLFGENAanskedifeiyyaDSGDNSNPLGSLNNN-----NGYANFRVSADIIDKLDGYGDPR------- 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825945 322 apggldsalvedpaqqrgmpngfdnneLAASNEYtddldqytrihpnlrdrndpmfFQTYAEVELMLAEAAVRGWNVpGS 401
Cdd:cd08977  275 ---------------------------LSLAPIP----------------------IIRYAEVLLLRAEALARLGNG-AD 304
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825945 402 AEAHYEAGVRAAmnyitrYGENTSVSDSEITQylsdnslpsgrEARLRAINNQYWAATFLNGIeSWSNWRRSG 474
Cdd:cd08977  305 AIEYLNAVRRRS------GGNAANNTSQASTA-----------EELLEEILDERRLELFGEGH-RWYDLRRTG 359
 
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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