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Conserved domains on  [gi|1681035553|dbj|BBK86169|]
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hypothetical protein Bun01g_05390 [Bacteroides uniformis]

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 ...
34-533 4.64e-39

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: 147.93  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553  34 PSKVTQVTISNLMVGVFQKVKDYDVYEYNRFFGFDSQFtGKYAQTFGYSNTTDMYTPGyipaiDGQWDNVYS-ALAQFRK 112
Cdd:pfam12771   1 PNAPTEITPGTLLTNALYNLANNNTNENYNINRLLMQY-WTPTTYGDESRYDFTRNIG-----NSFWNGYYRwVLKNLKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 113 LESLYEEESAAEQAQDeafYLA-AKVQLYDFFAATVDVFGDMPFSEACtlpltNDVGKSYAHYDKAEDIYKTILDELKEI 191
Cdd:pfam12771  75 MKNLAKEEAIDNANNN---YIAvALILKAYVYSNLTDTFGDVPYSEAL-----RGEEGLQPKYDSQEDIYKDLLADLDEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 192 APRFRsipTPRNFNTQDFINNGDMDKWERYANSLRLRLAMRVAaqgDLQ-AEGRTAIKEILENpsAYPLIEEQENNILIV 270
Cdd:pfam12771 147 NALYD---TGMGYNAGDILYNGDVEKWKKFANSLRLRMLLRIS---KVDpAKAKTEFESAIAA--GYPVFESNADNALLP 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 271 NQKSG-QLNFTAGHGLG---DWVtnrlASGAIIDRMLGHGnydmtsndplsgvyvkgedDPRILLNFNPVKITNQntgql 346
Cdd:pfam12771 219 YTGSTpNENPWYNLLVTraqDFA----MSAFFVDELNGLN-------------------DPRLPVFFTPNNIIGE----- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 347 dehrYLGtdltvadeltEYYNSQAQDEVNTSNTGFSQITQKgffwendKFDMLIMASPEIHFLKAESYEMGYGVAKNeak 426
Cdd:pfam12771 271 ----YVG----------VPYGYVGDNSYFDYSTSGDNVIQV-------TAPMVLLTYSEVEFILAEAAQRGWNISGT--- 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 427 AEEEFKKAVSQSITLYYyydsvsTGENARRYNAPTAeetASFAAAKWnsteyadkLDAIITQKWLHFgFLASREAWSDIR 506
Cdd:pfam12771 327 AAEHYNKGIKASIEQWG------GAADPAAYLAQPA---VAYNTATG--------LEKIGLQKWLAL-YFRGYEAWFEWR 388
                         490       500
                  ....*....|....*....|....*....
gi 1681035553 507 RTGYPSgLAfPEVAGTITN--VPNRWRYP 533
Cdd:pfam12771 389 RTGFPK-LP-PTGDGELNNgvIPVRLLYP 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 ...
34-533 4.64e-39

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: 147.93  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553  34 PSKVTQVTISNLMVGVFQKVKDYDVYEYNRFFGFDSQFtGKYAQTFGYSNTTDMYTPGyipaiDGQWDNVYS-ALAQFRK 112
Cdd:pfam12771   1 PNAPTEITPGTLLTNALYNLANNNTNENYNINRLLMQY-WTPTTYGDESRYDFTRNIG-----NSFWNGYYRwVLKNLKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 113 LESLYEEESAAEQAQDeafYLA-AKVQLYDFFAATVDVFGDMPFSEACtlpltNDVGKSYAHYDKAEDIYKTILDELKEI 191
Cdd:pfam12771  75 MKNLAKEEAIDNANNN---YIAvALILKAYVYSNLTDTFGDVPYSEAL-----RGEEGLQPKYDSQEDIYKDLLADLDEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 192 APRFRsipTPRNFNTQDFINNGDMDKWERYANSLRLRLAMRVAaqgDLQ-AEGRTAIKEILENpsAYPLIEEQENNILIV 270
Cdd:pfam12771 147 NALYD---TGMGYNAGDILYNGDVEKWKKFANSLRLRMLLRIS---KVDpAKAKTEFESAIAA--GYPVFESNADNALLP 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 271 NQKSG-QLNFTAGHGLG---DWVtnrlASGAIIDRMLGHGnydmtsndplsgvyvkgedDPRILLNFNPVKITNQntgql 346
Cdd:pfam12771 219 YTGSTpNENPWYNLLVTraqDFA----MSAFFVDELNGLN-------------------DPRLPVFFTPNNIIGE----- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 347 dehrYLGtdltvadeltEYYNSQAQDEVNTSNTGFSQITQKgffwendKFDMLIMASPEIHFLKAESYEMGYGVAKNeak 426
Cdd:pfam12771 271 ----YVG----------VPYGYVGDNSYFDYSTSGDNVIQV-------TAPMVLLTYSEVEFILAEAAQRGWNISGT--- 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 427 AEEEFKKAVSQSITLYYyydsvsTGENARRYNAPTAeetASFAAAKWnsteyadkLDAIITQKWLHFgFLASREAWSDIR 506
Cdd:pfam12771 327 AAEHYNKGIKASIEQWG------GAADPAAYLAQPA---VAYNTATG--------LEKIGLQKWLAL-YFRGYEAWFEWR 388
                         490       500
                  ....*....|....*....|....*....
gi 1681035553 507 RTGYPSgLAfPEVAGTITN--VPNRWRYP 533
Cdd:pfam12771 389 RTGFPK-LP-PTGDGELNNgvIPVRLLYP 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 ...
34-533 4.64e-39

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: 147.93  E-value: 4.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553  34 PSKVTQVTISNLMVGVFQKVKDYDVYEYNRFFGFDSQFtGKYAQTFGYSNTTDMYTPGyipaiDGQWDNVYS-ALAQFRK 112
Cdd:pfam12771   1 PNAPTEITPGTLLTNALYNLANNNTNENYNINRLLMQY-WTPTTYGDESRYDFTRNIG-----NSFWNGYYRwVLKNLKE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 113 LESLYEEESAAEQAQDeafYLA-AKVQLYDFFAATVDVFGDMPFSEACtlpltNDVGKSYAHYDKAEDIYKTILDELKEI 191
Cdd:pfam12771  75 MKNLAKEEAIDNANNN---YIAvALILKAYVYSNLTDTFGDVPYSEAL-----RGEEGLQPKYDSQEDIYKDLLADLDEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 192 APRFRsipTPRNFNTQDFINNGDMDKWERYANSLRLRLAMRVAaqgDLQ-AEGRTAIKEILENpsAYPLIEEQENNILIV 270
Cdd:pfam12771 147 NALYD---TGMGYNAGDILYNGDVEKWKKFANSLRLRMLLRIS---KVDpAKAKTEFESAIAA--GYPVFESNADNALLP 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 271 NQKSG-QLNFTAGHGLG---DWVtnrlASGAIIDRMLGHGnydmtsndplsgvyvkgedDPRILLNFNPVKITNQntgql 346
Cdd:pfam12771 219 YTGSTpNENPWYNLLVTraqDFA----MSAFFVDELNGLN-------------------DPRLPVFFTPNNIIGE----- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 347 dehrYLGtdltvadeltEYYNSQAQDEVNTSNTGFSQITQKgffwendKFDMLIMASPEIHFLKAESYEMGYGVAKNeak 426
Cdd:pfam12771 271 ----YVG----------VPYGYVGDNSYFDYSTSGDNVIQV-------TAPMVLLTYSEVEFILAEAAQRGWNISGT--- 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 427 AEEEFKKAVSQSITLYYyydsvsTGENARRYNAPTAeetASFAAAKWnsteyadkLDAIITQKWLHFgFLASREAWSDIR 506
Cdd:pfam12771 327 AAEHYNKGIKASIEQWG------GAADPAAYLAQPA---VAYNTATG--------LEKIGLQKWLAL-YFRGYEAWFEWR 388
                         490       500
                  ....*....|....*....|....*....
gi 1681035553 507 RTGYPSgLAfPEVAGTITN--VPNRWRYP 533
Cdd:pfam12771 389 RTGFPK-LP-PTGDGELNNgvIPVRLLYP 415
SusD-like pfam12741
Susd and RagB outer membrane lipoprotein; This is a family of SusD-like proteins, one member ...
61-558 1.33e-29

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: 122.00  E-value: 1.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553  61 YNRFFGFDSQFTgKYAQTFGYSNT--TDMYTpgyipaidgqwdNVYSALAQFRKleslyeeesAAEQAQDEAFYLAA--K 136
Cdd:pfam12741  59 PTNNFAGGNNNS-TYNLTEGWNNYpyDDAYP------------KVMSNWLEIKK---------ITEDPNPEFYALALilK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 137 VQLYdffAATVDVFGDMPFSEActlpltnDVGKSYAHYDKAEDIYKTILDELKE---IAPRFRSIPTPRNFNTqDFINNG 213
Cdd:pfam12741 117 VAAM---HRVTDIYGPIPYSKA-------GSGKLTVPYDSQEDVYKQFFKELDEaiaVLTPYRTAGFSSFPDY-DLVYGG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 214 DMDKWERYANSLRLRLAMRV--AAQGDLQAEGRTAIKeilenpSAYPLIEEQENNILIvnQKSGQLN--FTAGHGLGDwv 289
Cdd:pfam12741 186 DVEKWVKFANSLKLRLAMRIsyVDPALAKQYAEKAVN------HEIGVIETNDDNAKI--SSLTYKNplYTIANSYGD-- 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 290 tnrlasgaiiDRMlghgNYDMTSndplsgvYVKGEDDPRILLNFNPVKITNQNtgqldehRYLGTDLTVAdelteyYNSQ 369
Cdd:pfam12741 256 ----------TRM----GADIES-------YLNGYNDPRLEKYFTKSTFPDGG-------GYKGIRAGIN------IPSD 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 370 AQDEVNTSNTGFSQITQkgffwendkfdMLIMASPEIHFLKAESYEMGYGVAKNeakAEEEFKKAVSQSITLY------- 442
Cdd:pfam12741 302 KGAYRKYSKPNVTETTP-----------LYWMTAAEVAFLRAEGALRGWNMGGT---AKDLYEEGVTLSFEQWgvsgada 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681035553 443 YYYDSVSTGEN-----ARRYNAPTAEETASfaaAKWN---STEyaDKLDAIITQKWLHfGFLASREAWSDIRRTGYPSgl 514
Cdd:pfam12741 368 YLADSTSKPADytdplGPYYSAAGAPSTIT---IKWDdaaTNE--EKLERIITQKWIA-LFPNGQEAWSEFRRTGYPK-- 439
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1681035553 515 AFPEV----AGTITN--VPNRWRYPNTE-----VNYNPYYKEVSAEDTYYHKLFW 558
Cdd:pfam12741 440 LFPVAdnksGGVIDTerGIRRLPYPESEytnnkANYNKAVSLLGGPDNGGTRLWW 494
 
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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