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SUSD_BACO1
ID   SUSD_BACO1              Reviewed;         546 AA.
AC   A7LXT5;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=SusD-like protein BACOVA_02651;
DE   Flags: Precursor;
GN   ORFNames=BACOVA_02651;
OS   Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 /
OS   CCUG 4943 / NCTC 11153).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=411476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC
RC   11153;
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides ovatus (ATCC 8483).";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=24463512; DOI=10.1038/nature12907;
RA   Larsbrink J., Rogers T.E., Hemsworth G.R., McKee L.S., Tauzin A.S.,
RA   Spadiut O., Klinter S., Pudlo N.A., Urs K., Koropatkin N.M., Creagh A.L.,
RA   Haynes C.A., Kelly A.G., Cederholm S.N., Davies G.J., Martens E.C.,
RA   Brumer H.;
RT   "A discrete genetic locus confers xyloglucan metabolism in select human gut
RT   Bacteroidetes.";
RL   Nature 506:498-502(2014).
CC   -!- FUNCTION: Polysaccharide-binding protein present at the surface of the
CC       cell. Probably mediates xyloglucan-binding before xyloglucan transport
CC       in the periplasm for degradation. {ECO:0000269|PubMed:24463512}.
CC   -!- PATHWAY: Glucan metabolism; xyloglucan degradation.
CC       {ECO:0000269|PubMed:24463512}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}. Note=Cell outer membrane localization is predicted by
CC       analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
CC   -!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
CC       dietary polysaccharides through glycosidases that are absent in the
CC       human genome. Xyloglucans are a ubiquitous family of highly branched
CC       plant cell wall polysaccharides present in the vegetables we consume.
CC       Enzymes involved in xyloglucan degradation mediate the conversion of
CC       otherwise indigestible plant polysaccharides to short-chain fatty acids
CC       (PubMed:24463512). {ECO:0000305|PubMed:24463512}.
CC   -!- SIMILARITY: Belongs to the SusD family. {ECO:0000305}.
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DR   EMBL; AAXF02000049; EDO11442.1; -; Genomic_DNA.
DR   PDB; 5E75; X-ray; 1.36 A; A=28-546.
DR   PDB; 5E76; X-ray; 2.30 A; A=36-546.
DR   PDBsum; 5E75; -.
DR   PDBsum; 5E76; -.
DR   AlphaFoldDB; A7LXT5; -.
DR   SMR; A7LXT5; -.
DR   STRING; 411476.BACOVA_02651; -.
DR   EnsemblBacteria; EDO11442; EDO11442; BACOVA_02651.
DR   eggNOG; COG0561; Bacteria.
DR   HOGENOM; CLU_015553_1_3_10; -.
DR   UniPathway; UPA01045; -.
DR   Proteomes; UP000005475; Unassembled WGS sequence.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR   GO; GO:0085030; P:symbiotic process benefiting host; IDA:UniProtKB.
DR   GO; GO:2000899; P:xyloglucan catabolic process; IDA:UniProtKB.
DR   InterPro; IPR033985; SusD-like_N.
DR   InterPro; IPR012944; SusD_RagB_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF14322; SusD-like_3; 1.
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; Carbohydrate metabolism; Cell outer membrane; Lipoprotein;
KW   Membrane; Palmitate; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..546
FT                   /note="SusD-like protein BACOVA_02651"
FT                   /id="PRO_0000425884"
FT   LIPID           22
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           22
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   HELIX           44..51
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           67..71
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   TURN            72..76
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           97..122
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           130..152
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           178..195
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           207..222
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           232..248
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           257..261
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           263..265
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          271..275
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           290..293
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           297..299
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           313..318
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           324..330
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           343..345
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   TURN            365..368
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          382..386
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           387..399
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           409..420
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          427..429
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           431..442
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   TURN            443..446
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           448..458
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           460..468
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          477..481
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          487..492
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   STRAND          496..502
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           503..505
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           517..519
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           526..531
FT                   /evidence="ECO:0007829|PDB:5E75"
FT   HELIX           533..536
FT                   /evidence="ECO:0007829|PDB:5E75"
SQ   SEQUENCE   546 AA;  62096 MW;  8C3CF6641D560CDD CRC64;
     MRIFMKSKLL VIATTALLFA ACSDSFLDRA PEGNYVDATF YTSDEALEAA TAPLYNRAWF
     DYNQRSIVPI GSGRANDMYS PWNYPQFVTF QVTALDENLS GAWSGFYSVV TMANSVINAV
     ETQTQGSVSE AAKTKAIAEA RLMRACAYFY MLRIWGPVIL IEDNQKLVDN PVRPLNREED
     VFQFIINDLN YAVDNLSEQS DKGRATSWAA KGILAKVYLA RSGWNNGGTR DEGDLELARQ
     YASDVCENSG LDLMTNYEDL FKYKNNNNQE SLLAMQWVPL GEWYECNTLL SDLAFSTEVT
     GGVNCWSSYN GSIDMLQQYE LADTLRRNAT FFTKGSYYSY ICIKDGGYTY KGTASPIKKG
     VPGGPDDDND GKVKQMNSPL NTYILRLADV YLTYAEACLG NNSTLSDGRG LYFFNRVRER
     AKINKKSSIT LDDIIRERRV EFGMEYSNWY DMVTWFRYLP DKMLNYFNNQ WRGYRTDAII
     KDEDGKLHFG KYDTDGTTFL EGPEYYTAPE FTINIEAEDI FLPYPESDVI QNPLLNEPPV
     PYTFNE
 
 
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