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Conserved domains on  [gi|938483797|gb|ALJ48028|]
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SusD family protein [Bacteroides ovatus]

Protein Classification

RagB/SusD family nutrient uptake outer membrane protein( domain architecture ID 10172820)

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

Gene Ontology:  GO:0009279|GO:0016020
PubMed:  11717282|10986238

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SusD_RagB pfam07980
SusD family; This domain is found in bacterial cell surface proteins such SusD and SusD-like ...
 293-511 6.13e-38

SusD family; This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganizms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.


:

Pssm-ID: 429768  Cd Length: 294  Bit Score: 140.71  E-value: 6.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  293 KESILEAQFTPGAGNwcTWMFGRD--LVNWNNNF-----TWAkWVTPSRDLISTF----------------------KQE 343
Cdd:pfam07980   1 KESIFEVQYDSGVTG--GGGRSYGvnLGPNGGAGggeggGWG-GLGPTQDLVDLFymadgspifdtdddsdgtdtieIDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  344 GDEVRFKESVVYYDCGWSNYYP----------------------------SDNYPFMYKCRSANSSIIK----------Y 385
Cdd:pfam07980  78 NRDPRFYATVAFDGCTWNAGSNnlvyvagkytdgnlgsgdtgapnsdgnrSNTGYLLRKFVDEDGDSSGgggssidfpvI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  386 RYADVLLLKAEALIMQDtpDLEGAADIIDEVRDRAKLGALSSSTRSNKDALLNALLKERRLELAFEGQRWFDLVRLDKVE 465
Cdd:pfam07980 158 RYAEVLLNYAEALNELG--GPEEAIKYINKIRERAGLPDLTDSAYGSQEELIDAIRDERRIELAGEGHRFFDLRRWKKAL 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938483797  466 EVMNavhAKDSGRKAQVYTYDKNS----------------YRLPIPQSVIDANDKIHQNPGY 511
Cdd:pfam07980 236 QELN---GLFGGGNAYNGSNKGLDnfilerpdelednfkhYLLPIPQSEIDRNPGLTQNPGW 294
SusD cd08977
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
 54-460 4.47e-34

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: 131.77  E-value: 4.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  54 DKAAVESHLTTLYNQMRDRQEHWYVDLLLIAESHADNAYAGTTGAEVVPFENNSIEGSNSVLERDWNRYMEDVARANILI 133
Cdd:cd08977    1 DPTDAEAALTGLYAGLRSSGNYYGGTLGLLGDLRADD*VAASNSGDYTEVNTNNNPNDSAFGTSSWNGVYTNINNANIFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 134 CNIDAVTDnsLTTAERAQYKAEAKIFRAMIMFDMVRLWGDFPVITTVAEDITSdniedvypqyfPEQNTELEAYQQIERD 213
Cdd:cd08977   81 EKIDEASE--LTEANRNRYKGEAKFIRALAYFYLTRLFGGVPLSTAADQGTET-----------PPRDSQEEVYTQILAD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 214 LLDAVQYAPDNT-------PGNKTLFTKSVARTLLAKIY---AEKPLRDYTKVIQYCDEVKADGFDLVDDFSDLFGmnaa 283
Cdd:cd08977  148 LDEAIALLPEASsaqdfyiYFGDGRAWKKAARALLARVYlylANYTAADYAEALTAAEKSFKGGVTLLTNLFGENA---- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 284 gtdakmRNTKESILEAQFTPGAGNwctwmfGRDLVNWNNNFTWAKwVTPSRDLISTFKQEGDeVRFKesvvyydcgwsny 363
Cdd:cd08977  224 ------ANSKEDIFEIYYADSGDN------SNPLGSLNNNNGYAN-FRVSADIIDKLDGYGD-PRLS------------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 364 ypSDNYPFMykcrsanssiikyRYADVLLLKAEALIMQDtpDLEGAADIIDEVRDRA-KLGALSSSTRSNKDALLNALLK 442
Cdd:cd08977  277 --LAPIPII-------------RYAEVLLLRAEALARLG--NGADAIEYLNAVRRRSgGNAANNTSQASTAEELLEEILD 339

                        410
                 ....*....|....*...
gi 938483797 443 ERRLELAFEGQRWFDLVR 460
Cdd:cd08977  340 ERRLELFGEGHRWYDLRR 357
 
Name Accession Description Interval E-value
SusD_RagB pfam07980
SusD family; This domain is found in bacterial cell surface proteins such SusD and SusD-like ...
 293-511 6.13e-38

SusD family; This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganizms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.


Pssm-ID: 429768  Cd Length: 294  Bit Score: 140.71  E-value: 6.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  293 KESILEAQFTPGAGNwcTWMFGRD--LVNWNNNF-----TWAkWVTPSRDLISTF----------------------KQE 343
Cdd:pfam07980   1 KESIFEVQYDSGVTG--GGGRSYGvnLGPNGGAGggeggGWG-GLGPTQDLVDLFymadgspifdtdddsdgtdtieIDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  344 GDEVRFKESVVYYDCGWSNYYP----------------------------SDNYPFMYKCRSANSSIIK----------Y 385
Cdd:pfam07980  78 NRDPRFYATVAFDGCTWNAGSNnlvyvagkytdgnlgsgdtgapnsdgnrSNTGYLLRKFVDEDGDSSGgggssidfpvI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  386 RYADVLLLKAEALIMQDtpDLEGAADIIDEVRDRAKLGALSSSTRSNKDALLNALLKERRLELAFEGQRWFDLVRLDKVE 465
Cdd:pfam07980 158 RYAEVLLNYAEALNELG--GPEEAIKYINKIRERAGLPDLTDSAYGSQEELIDAIRDERRIELAGEGHRFFDLRRWKKAL 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938483797  466 EVMNavhAKDSGRKAQVYTYDKNS----------------YRLPIPQSVIDANDKIHQNPGY 511
Cdd:pfam07980 236 QELN---GLFGGGNAYNGSNKGLDnfilerpdelednfkhYLLPIPQSEIDRNPGLTQNPGW 294
SusD cd08977
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
 54-460 4.47e-34

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: 131.77  E-value: 4.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  54 DKAAVESHLTTLYNQMRDRQEHWYVDLLLIAESHADNAYAGTTGAEVVPFENNSIEGSNSVLERDWNRYMEDVARANILI 133
Cdd:cd08977    1 DPTDAEAALTGLYAGLRSSGNYYGGTLGLLGDLRADD*VAASNSGDYTEVNTNNNPNDSAFGTSSWNGVYTNINNANIFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 134 CNIDAVTDnsLTTAERAQYKAEAKIFRAMIMFDMVRLWGDFPVITTVAEDITSdniedvypqyfPEQNTELEAYQQIERD 213
Cdd:cd08977   81 EKIDEASE--LTEANRNRYKGEAKFIRALAYFYLTRLFGGVPLSTAADQGTET-----------PPRDSQEEVYTQILAD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 214 LLDAVQYAPDNT-------PGNKTLFTKSVARTLLAKIY---AEKPLRDYTKVIQYCDEVKADGFDLVDDFSDLFGmnaa 283
Cdd:cd08977  148 LDEAIALLPEASsaqdfyiYFGDGRAWKKAARALLARVYlylANYTAADYAEALTAAEKSFKGGVTLLTNLFGENA---- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 284 gtdakmRNTKESILEAQFTPGAGNwctwmfGRDLVNWNNNFTWAKwVTPSRDLISTFKQEGDeVRFKesvvyydcgwsny 363
Cdd:cd08977  224 ------ANSKEDIFEIYYADSGDN------SNPLGSLNNNNGYAN-FRVSADIIDKLDGYGD-PRLS------------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 364 ypSDNYPFMykcrsanssiikyRYADVLLLKAEALIMQDtpDLEGAADIIDEVRDRA-KLGALSSSTRSNKDALLNALLK 442
Cdd:cd08977  277 --LAPIPII-------------RYAEVLLLRAEALARLG--NGADAIEYLNAVRRRSgGNAANNTSQASTAEELLEEILD 339

                        410
                 ....*....|....*...
gi 938483797 443 ERRLELAFEGQRWFDLVR 460
Cdd:cd08977  340 ERRLELFGEGHRWYDLRR 357
SusD-like_3 pfam14322
Starch-binding associating with outer membrane; SusD is a secreted polysaccharide-binding ...
 103-241 6.57e-14

Starch-binding associating with outer membrane; SusD is a secreted polysaccharide-binding protein with an N-terminal lipid moiety that allows it to associate with the outer membrane. SusD probably mediates xyloglucan-binding prior to xyloglucan transport in the periplasm for degradation. This domain is found N-terminal to pfam07980.


Pssm-ID: 405073  Cd Length: 185  Bit Score: 70.13  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  103 FENNSIEGSNSVLERDWNRYMEDVARANILIcniDAVTDNSLTTAERAQYKAEAKIFRAMIMFDMVRLWGDFPVITTVAE 182
Cdd:pfam14322  60 EAYDDETITAATVTNDWSKYYKGIFTANTVL---ELLNSTEGTTEERNQVKGEALFLRAYAHFMLVNFFGGVPYTTATAA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938483797  183 DITSdniedvypqyfpEQNTELEAYQQIERDLLDAVQYAPDNT--PGNKTLFTKSVARTLL 241
Cdd:pfam14322 137 DVNL------------PRATVQEVYDKILKDLKEAIELLPDESeiIVPKTRPTKSAAYALL 185
 
Name Accession Description Interval E-value
SusD_RagB pfam07980
SusD family; This domain is found in bacterial cell surface proteins such SusD and SusD-like ...
 293-511 6.13e-38

SusD family; This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganizms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.


Pssm-ID: 429768  Cd Length: 294  Bit Score: 140.71  E-value: 6.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  293 KESILEAQFTPGAGNwcTWMFGRD--LVNWNNNF-----TWAkWVTPSRDLISTF----------------------KQE 343
Cdd:pfam07980   1 KESIFEVQYDSGVTG--GGGRSYGvnLGPNGGAGggeggGWG-GLGPTQDLVDLFymadgspifdtdddsdgtdtieIDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  344 GDEVRFKESVVYYDCGWSNYYP----------------------------SDNYPFMYKCRSANSSIIK----------Y 385
Cdd:pfam07980  78 NRDPRFYATVAFDGCTWNAGSNnlvyvagkytdgnlgsgdtgapnsdgnrSNTGYLLRKFVDEDGDSSGgggssidfpvI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  386 RYADVLLLKAEALIMQDtpDLEGAADIIDEVRDRAKLGALSSSTRSNKDALLNALLKERRLELAFEGQRWFDLVRLDKVE 465
Cdd:pfam07980 158 RYAEVLLNYAEALNELG--GPEEAIKYINKIRERAGLPDLTDSAYGSQEELIDAIRDERRIELAGEGHRFFDLRRWKKAL 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938483797  466 EVMNavhAKDSGRKAQVYTYDKNS----------------YRLPIPQSVIDANDKIHQNPGY 511
Cdd:pfam07980 236 QELN---GLFGGGNAYNGSNKGLDnfilerpdelednfkhYLLPIPQSEIDRNPGLTQNPGW 294
SusD cd08977
starch binding outer membrane protein SusD; SusD-like proteins from Bacteroidetes, members of ...
 54-460 4.47e-34

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: 131.77  E-value: 4.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  54 DKAAVESHLTTLYNQMRDRQEHWYVDLLLIAESHADNAYAGTTGAEVVPFENNSIEGSNSVLERDWNRYMEDVARANILI 133
Cdd:cd08977    1 DPTDAEAALTGLYAGLRSSGNYYGGTLGLLGDLRADD*VAASNSGDYTEVNTNNNPNDSAFGTSSWNGVYTNINNANIFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 134 CNIDAVTDnsLTTAERAQYKAEAKIFRAMIMFDMVRLWGDFPVITTVAEDITSdniedvypqyfPEQNTELEAYQQIERD 213
Cdd:cd08977   81 EKIDEASE--LTEANRNRYKGEAKFIRALAYFYLTRLFGGVPLSTAADQGTET-----------PPRDSQEEVYTQILAD 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 214 LLDAVQYAPDNT-------PGNKTLFTKSVARTLLAKIY---AEKPLRDYTKVIQYCDEVKADGFDLVDDFSDLFGmnaa 283
Cdd:cd08977  148 LDEAIALLPEASsaqdfyiYFGDGRAWKKAARALLARVYlylANYTAADYAEALTAAEKSFKGGVTLLTNLFGENA---- 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 284 gtdakmRNTKESILEAQFTPGAGNwctwmfGRDLVNWNNNFTWAKwVTPSRDLISTFKQEGDeVRFKesvvyydcgwsny 363
Cdd:cd08977  224 ------ANSKEDIFEIYYADSGDN------SNPLGSLNNNNGYAN-FRVSADIIDKLDGYGD-PRLS------------- 276

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797 364 ypSDNYPFMykcrsanssiikyRYADVLLLKAEALIMQDtpDLEGAADIIDEVRDRA-KLGALSSSTRSNKDALLNALLK 442
Cdd:cd08977  277 --LAPIPII-------------RYAEVLLLRAEALARLG--NGADAIEYLNAVRRRSgGNAANNTSQASTAEELLEEILD 339

                        410
                 ....*....|....*...
gi 938483797 443 ERRLELAFEGQRWFDLVR 460
Cdd:cd08977  340 ERRLELFGEGHRWYDLRR 357
SusD-like_3 pfam14322
Starch-binding associating with outer membrane; SusD is a secreted polysaccharide-binding ...
 103-241 6.57e-14

Starch-binding associating with outer membrane; SusD is a secreted polysaccharide-binding protein with an N-terminal lipid moiety that allows it to associate with the outer membrane. SusD probably mediates xyloglucan-binding prior to xyloglucan transport in the periplasm for degradation. This domain is found N-terminal to pfam07980.


Pssm-ID: 405073  Cd Length: 185  Bit Score: 70.13  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938483797  103 FENNSIEGSNSVLERDWNRYMEDVARANILIcniDAVTDNSLTTAERAQYKAEAKIFRAMIMFDMVRLWGDFPVITTVAE 182
Cdd:pfam14322  60 EAYDDETITAATVTNDWSKYYKGIFTANTVL---ELLNSTEGTTEERNQVKGEALFLRAYAHFMLVNFFGGVPYTTATAA 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938483797  183 DITSdniedvypqyfpEQNTELEAYQQIERDLLDAVQYAPDNT--PGNKTLFTKSVARTLL 241
Cdd:pfam14322 137 DVNL------------PRATVQEVYDKILKDLKEAIELLPDESeiIVPKTRPTKSAAYALL 185
 
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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