SUSC_BACTN
ID SUSC_BACTN Reviewed; 1003 AA.
AC Q8A1G1; Q45780;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=TonB-dependent receptor SusC;
DE AltName: Full=Starch-utilization system protein C;
DE Flags: Precursor;
GN Name=susC; OrderedLocusNames=BT_3702;
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], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8550519; DOI=10.1128/jb.178.3.823-830.1996;
RA Reeves A.R., D'Elia J.N., Frias J., Salyers A.A.;
RT "A Bacteroides thetaiotaomicron outer membrane protein that is essential
RT for utilization of maltooligosaccharides and starch.";
RL J. Bacteriol. 178:823-830(1996).
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.
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 [4]
RP FUNCTION.
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 [5]
RP FUNCTION, AND INTERACTION WITH SUSD.
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).
CC -!- FUNCTION: Mediates transport of starch oligosaccharides from the
CC surface of the outer membrane to the periplasm for subsequent
CC degradation. {ECO:0000269|PubMed:10986238, ECO:0000269|PubMed:11717282,
CC ECO:0000269|PubMed:8550519, ECO:0000269|PubMed:9006015}.
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBUNIT: Interacts with SusD. {ECO:0000269|PubMed:11717282}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By maltose. {ECO:0000269|PubMed:8550519}.
CC -!- DISRUPTION PHENOTYPE: Abolished ability to grow on starch.
CC {ECO:0000269|PubMed:8550519}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA95938.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L49338; AAA95938.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE015928; AAO78807.1; -; Genomic_DNA.
DR PIR; JC6027; JC6027.
DR RefSeq; NP_812613.1; NC_004663.1.
DR RefSeq; WP_011108938.1; NC_004663.1.
DR AlphaFoldDB; Q8A1G1; -.
DR SMR; Q8A1G1; -.
DR STRING; 226186.BT_3702; -.
DR TCDB; 1.B.14.6.1; the outer membrane receptor (omr) family.
DR PaxDb; Q8A1G1; -.
DR PRIDE; Q8A1G1; -.
DR EnsemblBacteria; AAO78807; AAO78807; BT_3702.
DR KEGG; bth:BT_3702; -.
DR PATRIC; fig|226186.12.peg.3762; -.
DR eggNOG; COG1629; Bacteria.
DR eggNOG; COG4206; Bacteria.
DR HOGENOM; CLU_004317_0_2_10; -.
DR InParanoid; Q8A1G1; -.
DR OMA; LNPDDRW; -.
DR UniPathway; UPA00153; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019867; C:outer membrane; IDA:MENGO.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:2001070; F:starch binding; IDA:MENGO.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR023996; TonB-dep_OMP_SusC/RagA.
DR InterPro; IPR023997; TonB-dep_OMP_SusC/RagA_CS.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR TIGRFAMs; TIGR04056; OMP_RagA_SusC; 1.
DR TIGRFAMs; TIGR04057; SusC_RagA_signa; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell outer membrane; Membrane; Receptor;
KW Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1003
FT /note="TonB-dependent receptor SusC"
FT /id="PRO_0000425882"
FT CONFLICT 249
FT /note="S -> T (in Ref. 1; AAA95938)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="A -> G (in Ref. 1; AAA95938)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="I -> ISRGNNTKVQAHKVGYAANSFYV (in Ref. 1; AAA95938)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="L -> F (in Ref. 1; AAA95938)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="D -> DY (in Ref. 1; AAA95938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 111144 MW; 93C1A907E1CD813B CRC64;
MKKGNFMFKV LLMLIAGIFL SIDAFAQQIT VKGIVKDTTG EPVIGANVVV KGTTTGTITD
FDGNFQLSAK QGDIIVVSFI GYQPQELPVA AQMNVILKDD TEILDEVVVI GYGQVKKNDM
TGSVMAIKPD ELSKGITTNA QDMLSGKIAG VSVISNDGTP GGGAQIRIRG GSSLNASNDP
LIVIDGLAID NEGIKGMANG LSMVNPADIE TLTVLKDASA TAIYGSRASN GVIIITTKKG
KNGQAPSVSY NGSVSFSKTQ KRYDVLSGDE YRAYANQLWG DKLPADLGTA NTDWQDQIFR
TAVSTDHHVS INGGFKNLPY RVSLGYTDDN GIVKTSNFRR FTASVNLAPS FFEDHLKFNI
NAKFMNGKNR YADTGAAIGG ALAIDPTRPV YSNEDPYQFT GGYWQNINST TGFSNPDWKY
TSNPNSPQNP LAALELKNDK ANSNDFVGNV DVDYKFHFLP DLRLHASIGG EYAEGTQTTI
VSPYSFGNNY YGWNGDVTQY KYNLSYNIYV QYIKSLGAND FDIMVGGEEQ HFHRNGFEEG
QGWDSYTQEP HDAKLREQTA YATRNTLVSY FGRLNYSLLN RYLFTFTMRW DGSSRFSKDN
RWGTFPSLAL GWKIKEENFL KDVNVLSDLK LRLGWGITGQ QNIGDDFAYL PLYVVNNEYA
QYPFGDTYYS TSRPKAFNEN LKWEKTTTWN AGLDFGFLNG RITGGIDGYF RKTDDLLNSV
KIPVGTNFNA QMTQNIGSLE NYGMEFSINA KPIVTKDFTW DLSYNITWNH NEITKLTGGD
DSDYYVEAGD KISRGNNTKV QAHKVGYAAN SFYVYQQVYD ENGKPIENMF VDRNGNGTID
SGDKYIYKKP AGDVLMGLTS KMQYKNFDFS FSLRASLNNY VYYDFLSNKA NVSTSGLFSN
NAYSNTSAEA VALGLSGQGD YMSDYFIHNA SFLRCDNITL GYSFQNLWKT QTYKGVGGRV
YATVQNPFII SKYKGLDPEV KSGIDANPYP RAMTFLLGLS LQF
