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Outer membrane protein SusF (Starch-utilization system protein F)

 SUSF_BACTN              Reviewed;         485 AA.
G8JZS6; Q45771; Q7C3Z4;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 1.
10-OCT-2018, entry version 36.
RecName: Full=Outer membrane protein SusF;
AltName: Full=Starch-utilization system protein F;
Flags: Precursor;
Name=susF; OrderedLocusNames=BT_3699;
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
10582 / E50 / VPI-5482).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=226186;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
PubMed=9006015; DOI=10.1128/jb.179.3.643-649.1997;
Reeves A.R., Wang G.R., Salyers A.A.;
"Characterization of four outer membrane proteins that play a role in
utilization of starch by Bacteroides thetaiotaomicron.";
J. Bacteriol. 179:643-649(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
PubMed=12663928; DOI=10.1126/science.1080029;
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).
[3]
FUNCTION, AND INTERACTION WITH SUSF.
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
PubMed=11717282; DOI=10.1128/JB.183.24.7224-7230.2001;
Cho K.H., Salyers A.A.;
"Biochemical analysis of interactions between outer membrane proteins
that contribute to starch utilization by Bacteroides
thetaiotaomicron.";
J. Bacteriol. 183:7224-7230(2001).
[4]
FUNCTION, AND STARCH-BINDING.
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
PubMed=10986238; DOI=10.1128/JB.182.19.5365-5372.2000;
Shipman J.A., Berleman J.E., Salyers A.A.;
"Characterization of four outer membrane proteins involved in binding
starch to the cell surface of Bacteroides thetaiotaomicron.";
J. Bacteriol. 182:5365-5372(2000).
[5]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 21-485 IN COMPLEX WITH
ALPHA-D-GLUCOSE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
STARCH-BINDING, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20,
AND MUTAGENESIS OF CYS-20; TRP-177; LYS-208; TRP-222; ASP-231;
TRP-287; LYS-323; ASN-356; TRP-396; TRP-442 AND ARG-456.
PubMed=22910908; DOI=10.1074/jbc.M112.397380;
Cameron E.A., Maynard M.A., Smith C.J., Smith T.J., Koropatkin N.M.,
Martens E.C.;
"Multidomain carbohydrate-binding proteins involved in bacteroides
thetaiotaomicron starch metabolism.";
J. Biol. Chem. 287:34614-34625(2012).
-!- FUNCTION: Starch-binding protein present at the surface of the
cell. Mediates starch-binding before starch transport in the
periplasm for degradation. SusE and SusF do not constitute the
major starch-binding proteins in starch degradation pathway. Has
lower affinity for starch compared to SusE.
{ECO:0000269|PubMed:10986238, ECO:0000269|PubMed:11717282,
ECO:0000269|PubMed:22910908}.
-!- PATHWAY: Glycan degradation; starch degradation.
-!- SUBUNIT: Monomer (Probable). Interacts with SusE.
{ECO:0000269|PubMed:11717282, ECO:0000269|PubMed:22910908,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:22910908}; Lipid-anchor {ECO:0000255|PROSITE-
ProRule:PRU00303, ECO:0000269|PubMed:22910908}.
-!- INDUCTION: By maltose. {ECO:0000269|PubMed:9006015}.
-!- DOMAIN: The carbohydrate binding modules (CBM) mediate starch-
binding. {ECO:0000269|PubMed:22910908}.
-!- SIMILARITY: Belongs to the SusF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L77733; AAB42173.1; -; Genomic_DNA.
EMBL; AE015928; AAO78804.1; -; Genomic_DNA.
RefSeq; NP_812610.1; NC_004663.1.
RefSeq; WP_008767007.1; NC_004663.1.
PDB; 4FE9; X-ray; 2.00 A; A=21-485.
PDBsum; 4FE9; -.
SMR; G8JZS6; -.
STRING; 226186.BT_3699; -.
TCDB; 1.B.38.4.2; the treponema porin major surface protein (tp-msp) family.
PaxDb; G8JZS6; -.
PRIDE; G8JZS6; -.
EnsemblBacteria; AAO78804; AAO78804; BT_3699.
GeneID; 1072051; -.
GeneID; 31618993; -.
KEGG; bth:BT_3699; -.
PATRIC; fig|226186.12.peg.3759; -.
eggNOG; ENOG4106JX8; Bacteria.
eggNOG; ENOG410YAEF; LUCA.
KO; K21571; -.
OrthoDB; POG091H0JJ6; -.
BioCyc; BTHE:G13PU-8667-MONOMER; -.
UniPathway; UPA00153; -.
Proteomes; UP000001414; Chromosome.
GO; GO:0009279; C:cell outer membrane; IDA:UniProtKB.
GO; GO:0019867; C:outer membrane; IDA:MENGO.
GO; GO:2001070; F:starch binding; IDA:UniProtKB.
GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0005982; P:starch metabolic process; IDA:UniProtKB.
InterPro; IPR033408; DUF5115.
InterPro; IPR032187; SusF/SusE.
Pfam; PF17142; DUF5115; 1.
Pfam; PF16411; SusF_SusE; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Cell outer membrane;
Complete proteome; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal.
SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 20 485 Outer membrane protein SusF.
/FTId=PRO_0000425890.
REGION 161 274 Carbohydrate binding module (CBM) 1.
REGION 206 208 Glucose binding.
REGION 275 383 Carbohydrate binding module (CBM) 2.
REGION 384 485 Carbohydrate binding module (CBM) 3.
BINDING 173 173 Glucose.
BINDING 231 231 Glucose.
LIPID 20 20 N-palmitoyl cysteine.
{ECO:0000305|PubMed:22910908}.
LIPID 20 20 S-diacylglycerol cysteine.
{ECO:0000305|PubMed:22910908}.
MUTAGEN 20 20 C->A: Abolishes cell outer membrane
localization.
{ECO:0000269|PubMed:22910908}.
MUTAGEN 177 177 W->A: Abolished binding to starch; when
associated with A-208; A-222; A-231; A-
287; A-323; A-356; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 208 208 K->A: Abolished binding to starch; when
associated with A-177; A-222; A-231; A-
287; A-323; A-356; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 222 222 W->A: Abolished binding to starch; when
associated with A-177; A-208; A-231; A-
287; A-323; A-356; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 231 231 D->A: Abolished binding to starch; when
associated with A-177; A-208; A-222; A-
287; A-323; A-356; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 287 287 W->A: Abolished binding to starch; when
associated with A-177; A-208; A-222; A-
231; A-323; A-356; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 323 323 K->A: Abolished binding to starch; when
associated with A-177; A-208; A-222; A-
231; A-287; A-356; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 356 356 N->A: Abolished binding to starch; when
associated with A-177; A-208; A-222; A-
231; A-287; A-323; A-396; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 396 396 W->A: Abolished binding to starch; when
associated with A-177; A-208; A-222; A-
231; A-287; A-323; A-356; A-442 and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 442 442 W->A: Abolished binding to starch; when
associated with A-177; A-208; A-222; A-
231; A-287; A-323; A-356; A-396; and A-
456. {ECO:0000269|PubMed:22910908}.
MUTAGEN 456 456 R->A: Abolished binding to starch; when
associated with A-287; A-323; A-356; A-
396 and A-442.
{ECO:0000269|PubMed:22910908}.
STRAND 42 48 {ECO:0000244|PDB:4FE9}.
STRAND 53 55 {ECO:0000244|PDB:4FE9}.
HELIX 56 58 {ECO:0000244|PDB:4FE9}.
STRAND 62 74 {ECO:0000244|PDB:4FE9}.
STRAND 79 87 {ECO:0000244|PDB:4FE9}.
TURN 88 90 {ECO:0000244|PDB:4FE9}.
STRAND 102 106 {ECO:0000244|PDB:4FE9}.
HELIX 107 117 {ECO:0000244|PDB:4FE9}.
STRAND 126 137 {ECO:0000244|PDB:4FE9}.
STRAND 143 147 {ECO:0000244|PDB:4FE9}.
STRAND 151 156 {ECO:0000244|PDB:4FE9}.
STRAND 168 172 {ECO:0000244|PDB:4FE9}.
TURN 173 175 {ECO:0000244|PDB:4FE9}.
HELIX 179 181 {ECO:0000244|PDB:4FE9}.
STRAND 194 203 {ECO:0000244|PDB:4FE9}.
STRAND 206 211 {ECO:0000244|PDB:4FE9}.
HELIX 212 214 {ECO:0000244|PDB:4FE9}.
HELIX 222 224 {ECO:0000244|PDB:4FE9}.
STRAND 226 230 {ECO:0000244|PDB:4FE9}.
STRAND 236 239 {ECO:0000244|PDB:4FE9}.
STRAND 254 261 {ECO:0000244|PDB:4FE9}.
TURN 262 265 {ECO:0000244|PDB:4FE9}.
STRAND 266 271 {ECO:0000244|PDB:4FE9}.
STRAND 279 282 {ECO:0000244|PDB:4FE9}.
HELIX 283 288 {ECO:0000244|PDB:4FE9}.
TURN 294 296 {ECO:0000244|PDB:4FE9}.
STRAND 309 316 {ECO:0000244|PDB:4FE9}.
STRAND 321 332 {ECO:0000244|PDB:4FE9}.
HELIX 342 348 {ECO:0000244|PDB:4FE9}.
STRAND 351 353 {ECO:0000244|PDB:4FE9}.
STRAND 356 358 {ECO:0000244|PDB:4FE9}.
STRAND 363 372 {ECO:0000244|PDB:4FE9}.
STRAND 375 381 {ECO:0000244|PDB:4FE9}.
STRAND 386 389 {ECO:0000244|PDB:4FE9}.
HELIX 395 397 {ECO:0000244|PDB:4FE9}.
HELIX 402 404 {ECO:0000244|PDB:4FE9}.
STRAND 422 430 {ECO:0000244|PDB:4FE9}.
HELIX 438 444 {ECO:0000244|PDB:4FE9}.
STRAND 445 449 {ECO:0000244|PDB:4FE9}.
STRAND 452 455 {ECO:0000244|PDB:4FE9}.
STRAND 472 476 {ECO:0000244|PDB:4FE9}.
TURN 477 480 {ECO:0000244|PDB:4FE9}.
STRAND 481 485 {ECO:0000244|PDB:4FE9}.
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


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