SUSF_BACTN
ID SUSF_BACTN Reviewed; 485 AA.
AC G8JZS6; Q45771; Q7C3Z4;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Outer membrane protein SusF;
DE AltName: Full=Starch-utilization system protein F;
DE Flags: Precursor;
GN Name=susF; OrderedLocusNames=BT_3699;
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 (2.00 ANGSTROMS) OF 21-485 IN COMPLEX WITH
RP ALPHA-D-GLUCOSE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, STARCH-BINDING,
RP DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20, AND MUTAGENESIS OF
RP CYS-20; TRP-177; LYS-208; TRP-222; ASP-231; TRP-287; LYS-323; ASN-356;
RP TRP-396; TRP-442 AND ARG-456.
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 lower affinity for starch
CC compared to SusE. {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 SusE.
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 SusF family. {ECO:0000305}.
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DR EMBL; L77733; AAB42173.1; -; Genomic_DNA.
DR EMBL; AE015928; AAO78804.1; -; Genomic_DNA.
DR RefSeq; NP_812610.1; NC_004663.1.
DR RefSeq; WP_008767007.1; NC_004663.1.
DR PDB; 4FE9; X-ray; 2.00 A; A=21-485.
DR PDBsum; 4FE9; -.
DR AlphaFoldDB; G8JZS6; -.
DR SMR; G8JZS6; -.
DR STRING; 226186.BT_3699; -.
DR TCDB; 1.B.38.4.2; the treponema porin major surface protein (tp-msp) family.
DR PaxDb; G8JZS6; -.
DR PRIDE; G8JZS6; -.
DR DNASU; 1072051; -.
DR EnsemblBacteria; AAO78804; AAO78804; BT_3699.
DR GeneID; 60924868; -.
DR KEGG; bth:BT_3699; -.
DR PATRIC; fig|226186.12.peg.3759; -.
DR eggNOG; ENOG5033Q7G; Bacteria.
DR HOGENOM; CLU_042892_1_0_10; -.
DR UniPathway; UPA00153; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
DR GO; GO:0019867; C:outer membrane; IDA:MENGO.
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; IDA:UniProtKB.
DR InterPro; IPR033408; DUF5115.
DR InterPro; IPR032187; SusF/SusE.
DR Pfam; PF17142; DUF5115; 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..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..485
FT /note="Outer membrane protein SusF"
FT /id="PRO_0000425890"
FT REGION 161..274
FT /note="Carbohydrate binding module (CBM) 1"
FT REGION 275..383
FT /note="Carbohydrate binding module (CBM) 2"
FT REGION 384..485
FT /note="Carbohydrate binding module (CBM) 3"
FT BINDING 173
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT BINDING 206..208
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT BINDING 231
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:22910908"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:22910908"
FT MUTAGEN 20
FT /note="C->A: Abolishes cell outer membrane localization."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 177
FT /note="W->A: Abolished binding to starch; when associated
FT with A-208; A-222; A-231; A-287; A-323; A-356; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 208
FT /note="K->A: Abolished binding to starch; when associated
FT with A-177; A-222; A-231; A-287; A-323; A-356; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 222
FT /note="W->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-231; A-287; A-323; A-356; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 231
FT /note="D->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-222; A-287; A-323; A-356; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 287
FT /note="W->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-222; A-231; A-323; A-356; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 323
FT /note="K->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-222; A-231; A-287; A-356; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 356
FT /note="N->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-222; A-231; A-287; A-323; A-396; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 396
FT /note="W->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-222; A-231; A-287; A-323; A-356; A-442
FT and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 442
FT /note="W->A: Abolished binding to starch; when associated
FT with A-177; A-208; A-222; A-231; A-287; A-323; A-356; A-
FT 396; and A-456."
FT /evidence="ECO:0000269|PubMed:22910908"
FT MUTAGEN 456
FT /note="R->A: Abolished binding to starch; when associated
FT with A-287; A-323; A-356; A-396 and A-442."
FT /evidence="ECO:0000269|PubMed:22910908"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:4FE9"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 126..137
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4FE9"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:4FE9"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:4FE9"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 321..332
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:4FE9"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:4FE9"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:4FE9"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:4FE9"
SQ SEQUENCE 485 AA; 52125 MW; 5718270A7A167127 CRC64;
MKKHLIYTGM FLAAIGFSAC NEDFKDWADP QSNPQEESAG QLTATFTAGK DASIVMDAAT
ADSVEIAKLS STTAEEGSKI AVNSLTLNEN HTIPFSMTED HVFKVALAQL DSVTQEAYKS
RASVVRELKI SINASAVTPS GEGIQLVGNE VSITLQPATT PAVDPDGYYI VGDFTGWDGN
SAQQMKKDAL DENLYILEAE IESTSNFKIF PASAINGNDI DWTKALGSSV DGDDSGDNFV
SWTNAGAINT ALDGKIKISF DAFNYRFTVK DNSAPTELYM TGSAYNWGTP AGDPNAWKAL
VPVNGTKGTF WGIFYFAAND QVKFAPQANW GNDFGFVDAI SQESKDLAGL SDEGGNLKVG
IAGWYLVYVS VIGDDKVIEF EKPNVYLMGD TSYNGWDAQL VEQDLFTVPG TADGEFVSPA
FLKDGAVRIC VNPKAVSAGD WWKTEFIIFD GQIAYRGNGG DQAAVQGKTG QKVYLNFGNG
TGRIE
