ID SUSD_BACTN Reviewed; 551 AA. AC Q8A1G2; Q45770; DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Starch-binding protein SusD; DE AltName: Full=Starch-utilization system protein D; DE Flags: Precursor; GN Name=susD; OrderedLocusNames=BT_3701; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND SUBCELLULAR RP LOCATION. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=9006015; DOI=10.1128/jb.179.3.643-649.1997; RA Reeves A.R., Wang G.R., Salyers A.A.; RT "Characterization of four outer membrane proteins that play a role in RT utilization of starch by Bacteroides thetaiotaomicron."; RL J. Bacteriol. 179:643-649(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., RA Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). RN [3] RP FUNCTION, STARCH-BINDING, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=10986238; DOI=10.1128/jb.182.19.5365-5372.2000; RA Shipman J.A., Berleman J.E., Salyers A.A.; RT "Characterization of four outer membrane proteins involved in binding RT starch to the cell surface of Bacteroides thetaiotaomicron."; RL J. Bacteriol. 182:5365-5372(2000). RN [4] RP FUNCTION, AND INTERACTION WITH SUSC. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50; RX PubMed=11717282; DOI=10.1128/jb.183.24.7224-7230.2001; RA Cho K.H., Salyers A.A.; RT "Biochemical analysis of interactions between outer membrane proteins that RT contribute to starch utilization by Bacteroides thetaiotaomicron."; RL J. Bacteriol. 183:7224-7230(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 26-551 IN COMPLEXES WITH CALCIUM RP AND MALTOHEPTAOSE, FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE. RX PubMed=18611383; DOI=10.1016/j.str.2008.03.017; RA Koropatkin N.M., Martens E.C., Gordon J.I., Smith T.J.; RT "Starch catabolism by a prominent human gut symbiont is directed by the RT recognition of amylose helices."; RL Structure 16:1105-1115(2008). CC -!- FUNCTION: Major starch-binding protein present at the surface of the CC cell. Mediates starch-binding before starch transport in the periplasm CC for degradation. {ECO:0000269|PubMed:10986238, CC ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:18611383, CC ECO:0000269|PubMed:9006015}. CC -!- PATHWAY: Glycan degradation; starch degradation. CC -!- SUBUNIT: Interacts with SusC. {ECO:0000269|PubMed:11717282, CC ECO:0000269|PubMed:18611383}. CC -!- INTERACTION: CC Q8A1G2; Q8A1G2: susD; NbExp=3; IntAct=EBI-15714708, EBI-15714708; CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:10986238, CC ECO:0000305|PubMed:9006015}; Lipid-anchor {ECO:0000305|PubMed:10986238, CC ECO:0000305|PubMed:9006015}. CC -!- INDUCTION: By maltose. {ECO:0000269|PubMed:9006015}. CC -!- DOMAIN: The binding pocket contains an arc of aromatic residues that CC complements the natural helical structure of starch and imposes this CC conformation on bound maltoheptaose. Binds cyclic oligosaccharides with CC higher affinity than linear forms (PubMed:18611383). CC {ECO:0000269|PubMed:18611383}. CC -!- DISRUPTION PHENOTYPE: Abolished ability to grow on amylopectin and CC pullulan, as well as maltohexaose and maltoheptaose. CC {ECO:0000269|PubMed:18611383}. CC -!- SIMILARITY: Belongs to the SusD family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB42172.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L77614; AAB42172.1; ALT_FRAME; Genomic_DNA. DR EMBL; AE015928; AAO78806.1; -; Genomic_DNA. DR RefSeq; NP_812612.1; NC_004663.1. DR RefSeq; WP_008767005.1; NC_004663.1. DR PDB; 3CK7; X-ray; 2.10 A; A/B/C/D=26-551. DR PDB; 3CK8; X-ray; 2.10 A; A/B=26-551. DR PDB; 3CK9; X-ray; 2.20 A; A/B=26-551. DR PDB; 3CKB; X-ray; 2.30 A; A/B=26-551. DR PDB; 3CKC; X-ray; 1.50 A; A/B=26-551. DR PDBsum; 3CK7; -. DR PDBsum; 3CK8; -. DR PDBsum; 3CK9; -. DR PDBsum; 3CKB; -. DR PDBsum; 3CKC; -. DR AlphaFoldDB; Q8A1G2; -. DR SMR; Q8A1G2; -. DR DIP; DIP-46026N; -. DR STRING; 226186.BT_3701; -. DR TCDB; 8.A.46.1.1; the glycan-binding protein (susd) family. DR PaxDb; 226186-BT_3701; -. DR EnsemblBacteria; AAO78806; AAO78806; BT_3701. DR GeneID; 60924870; -. DR KEGG; bth:BT_3701; -. DR PATRIC; fig|226186.12.peg.3761; -. DR eggNOG; COG3637; Bacteria. DR HOGENOM; CLU_015553_1_2_10; -. DR InParanoid; Q8A1G2; -. DR OrthoDB; 5694214at2; -. DR UniPathway; UPA00153; -. DR EvolutionaryTrace; Q8A1G2; -. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019867; C:outer membrane; IDA:MENGO. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:2001070; F:starch binding; IDA:UniProtKB. DR GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005982; P:starch metabolic process; IMP:UniProtKB. DR CDD; cd08977; SusD; 1. DR Gene3D; 1.25.40.390; -; 1. DR Gene3D; 1.10.3780.10; SusD-like; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR012944; SusD_RagB_dom. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR NCBIfam; NF033071; SusD; 1. DR Pfam; PF07980; SusD_RagB; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Cell outer membrane; KW Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome; KW Signal. FT SIGNAL 1..24 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 25..551 FT /note="Starch-binding protein SusD" FT /id="PRO_0000425883" FT BINDING 73..75 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 81 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 98..101 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 296 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 320 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 430 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 432 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT LIPID 25 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT LIPID 25 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CONFLICT 423 FT /note="V -> A (in Ref. 1; AAB42172)" FT /evidence="ECO:0000305" FT CONFLICT 481..482 FT /note="LI -> TNR (in Ref. 1; AAB42172)" FT /evidence="ECO:0000305" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:3CK8" FT HELIX 44..53 FT /evidence="ECO:0007829|PDB:3CKC" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:3CKC" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:3CK9" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:3CK9" FT TURN 74..77 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 79..88 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 91..97 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 104..109 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 117..139 FT /evidence="ECO:0007829|PDB:3CKC" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:3CK7" FT HELIX 146..170 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 185..188 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 189..203 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:3CKC" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:3CK8" FT HELIX 220..232 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 234..238 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 243..254 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 264..268 FT /evidence="ECO:0007829|PDB:3CKC" FT TURN 270..274 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 290..293 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 298..304 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 327..330 FT /evidence="ECO:0007829|PDB:3CKC" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 351..353 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 357..366 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 371..378 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 404..406 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 426..428 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 433..437 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 439..451 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 457..466 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 478..489 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 495..501 FT /evidence="ECO:0007829|PDB:3CKC" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 515..517 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 526..529 FT /evidence="ECO:0007829|PDB:3CKC" FT HELIX 535..540 FT /evidence="ECO:0007829|PDB:3CKC" SQ SEQUENCE 551 AA; 62309 MW; EBBB322E687A5E7F CRC64; MKTKYIKQLF SAALIAVLSS GVTSCINDLD ISPIDPQTGG SFDQQGVFVK GYAMLGVTGQ KGIDGSPDLD GQDEGESGFY RTTFNCNELP TDECLWAWQE NQDIPQLTSI SWSPSSQRTE WVYVRLGYDI TQYNFFLDQT EGMTDAETLR QRAEIRFLRA LHYWYFLDLF GKAPFKEHFS NDLPVEKKGT ELYTYIQNEL NEIEADMYEP RQAPFGRADK AANWLLRARL YLNAGVYTGQ TDYAKAEEYA SKVIGSAYKL CTNYSELFMA DNDENENAMQ EIILPIRQDG VKTRNYGGST YLVCGTRVAG MPRMGTTNGW SCIFARAAMV QKFFSNLEDV PMLPADVEIP TKGLDTDEQI DAFDAEHGIR TEDMIKAAGD DRALLYSGVG GGRRKIQTDA ISGFTDGLSI VKWQNYRSDG KPVSHATYPD TDIPLFRLAE AYLTRAEAIF RQGGDATGDI NELRKRANCT RKVQTVTEQE LIDEWAREFY LEGRRRSDLV RFGMFTTNKY LWDWKGGAMN GTSVASYYNK YPIPVSDINN NRNMSQNEGY K //