SUSE_BACTN
ID SUSE_BACTN Reviewed; 387 AA.
AC G8JZT0; Q45769; Q7C3Z3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Outer membrane protein SusE;
DE AltName: Full=Starch-utilization system protein E;
DE Flags: Precursor;
GN Name=susE; OrderedLocusNames=BT_3700;
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], AND INDUCTION.
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, AND INTERACTION WITH SUSF.
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 [4]
RP FUNCTION, AND STARCH-BINDING.
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 X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 35-387 IN COMPLEX WITH
RP ALPHA-D-GLUCOSE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, STARCH-BINDING,
RP DIACYLGLYCEROL AT CYS-21, PALMITOYLATION AT CYS-21, AND MUTAGENESIS OF
RP CYS-21; TRP-192; LYS-221; TYR-229; ASN-252; ARG-326; TRP-336 AND ARG-350.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=22910908; DOI=10.1074/jbc.m112.397380;
RA Cameron E.A., Maynard M.A., Smith C.J., Smith T.J., Koropatkin N.M.,
RA Martens E.C.;
RT "Multidomain carbohydrate-binding proteins involved in bacteroides
RT thetaiotaomicron starch metabolism.";
RL J. Biol. Chem. 287:34614-34625(2012).
CC -!- FUNCTION: Starch-binding protein present at the surface of the cell.
CC Mediates starch-binding before starch transport in the periplasm for
CC degradation. SusE and SusF do not constitute the major starch-binding
CC proteins in starch degradation pathway. Has higher affinity for starch
CC compared to SusF. {ECO:0000269|PubMed:10986238,
CC ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:22910908}.
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBUNIT: Monomer (Probable). Interacts with SusF.
CC {ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:22910908,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:22910908}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:22910908}.
CC -!- INDUCTION: By maltose. {ECO:0000269|PubMed:9006015}.
CC -!- DOMAIN: The carbohydrate binding modules (CBM) mediate starch-binding.
CC {ECO:0000269|PubMed:22910908}.
CC -!- SIMILARITY: Belongs to the SusE family. {ECO:0000305}.
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DR EMBL; L77615; AAB42171.1; -; Genomic_DNA.
DR EMBL; AE015928; AAO78805.1; -; Genomic_DNA.
DR RefSeq; NP_812611.1; NC_004663.1.
DR RefSeq; WP_008767006.1; NC_004663.1.
DR PDB; 4FCH; X-ray; 1.30 A; A/B=171-387.
DR PDB; 4FEM; X-ray; 2.50 A; A=35-387.
DR PDBsum; 4FCH; -.
DR PDBsum; 4FEM; -.
DR AlphaFoldDB; G8JZT0; -.
DR SMR; G8JZT0; -.
DR STRING; 226186.BT_3700; -.
DR TCDB; 1.B.38.4.1; the treponema porin major surface protein (tp-msp) family.
DR PaxDb; G8JZT0; -.
DR PRIDE; G8JZT0; -.
DR DNASU; 1076278; -.
DR EnsemblBacteria; AAO78805; AAO78805; BT_3700.
DR GeneID; 60924869; -.
DR KEGG; bth:BT_3700; -.
DR PATRIC; fig|226186.12.peg.3760; -.
DR eggNOG; ENOG502Z9RZ; Bacteria.
DR HOGENOM; CLU_042892_1_0_10; -.
DR OMA; TCSQPDY; -.
DR UniPathway; UPA00153; -.
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:2001070; F:starch binding; IDA:MENGO.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR025970; SusE.
DR InterPro; IPR032187; SusF/SusE.
DR Pfam; PF14292; SusE; 1.
DR Pfam; PF16411; SusF_SusE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell outer membrane; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..387
FT /note="Outer membrane protein SusE"
FT /id="PRO_0000425889"
FT REGION 174..283
FT /note="Carbohydrate binding module (CBM) 1"
FT REGION 284..387
FT /note="Carbohydrate binding module (CBM) 2"
FT BINDING 326
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT BINDING 335
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT BINDING 350..355
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:22910908"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:22910908"
FT MUTAGEN 21
FT /note="C->A: Abolishes cell outer membrane localization."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 192
FT /note="W->A: Impaired binding to starch; when associated
FT with A-221; A-229 and A-252. Abolished binding to starch;
FT when associated with A-221; A-229; A-252; A-326; A-336 and
FT A-350."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 221
FT /note="K->A: Impaired binding to starch; when associated
FT with A-192; A-229 and A-252. Abolished binding to starch;
FT when associated with A-192; A-229; A-252; A-326; A-336 and
FT A-350."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 229
FT /note="Y->A: Impaired binding to starch; when associated
FT with A-192; A-221 and A-252. Abolished binding to starch;
FT when associated with A-192; A-221; A-252; A-326; A-336 and
FT A-350."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 252
FT /note="N->A: Impaired binding to starch; when associated
FT with A-192; A-221 and A-229. Abolished binding to starch;
FT when associated with A-192; A-221; A-229; A-326; A-336 and
FT A-350."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 326
FT /note="R->A: Impaired binding to starch; when associated
FT with A-336 and A-350. Abolished binding to starch; when
FT associated with A-192; A-221; A-229; A-252; A-336 and A-
FT 350."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 336
FT /note="W->A: Impaired binding to starch; when associated
FT with A-326 and A-350. Abolished binding to starch; when
FT associated with A-192; A-221; A-229; A-252; A-326; and A-
FT 350."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 350
FT /note="R->A: Impaired binding to starch; when associated
FT with A-326 and A-336. Abolished binding to starch; when
FT associated with A-192; A-221; A-229; A-252; A-326 and A-
FT 336."
FT /evidence="ECO:0000269|PubMed:22910908"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4FCH"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 273..282
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:4FCH"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4FCH"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:4FCH"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:4FCH"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:4FCH"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:4FCH"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:4FCH"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:4FCH"
SQ SEQUENCE 387 AA; 42755 MW; D6D0620E02BE6980 CRC64;
MKKISNILLA VTFALPLFTA CETDNDSNPI LNEPDTFTLN TPAYAANNVY DLKNAQTVEL
TCSQPDYGFP AATTYTVQAS FEQDFIEATD ESKANYTVLE STSPTAKINV DASELNNALL
DLWTAVNGEQ AELPTEPVAV YIRLKANITS SGKGVCFSNV IELPNVLISK STSSLTPPKT
MFIVGSMLDT DWKVWKPMAG VYGMDGQFYS MIYFDANSEF KFGTKENEYI GINDNRVTVT
DKAGAGVSGS DNFVVENAGW YLFYVKAAVK GDDYQFTITF YPAEVYLFGN TTGGSWAFND
EWKFTVPATK DGNFVSPAMT ASGEVRMCFK TDLDWWRTEF TLHDGEIFYR DFNLIDSWTE
KGDGYSIQGS AGNVIHLNFT AGTGEKK
