SUSD_BACTN
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 03-AUG-2022, entry version 109.
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; Bacteroidetes; 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};
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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; Q8A1G2; -.
DR PRIDE; Q8A1G2; -.
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 OMA; DEWSREF; -.
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 Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR012944; SusD_RagB_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF07980; SusD_RagB; 1.
DR SUPFAM; SSF48452; SSF48452; 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
