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BCSA_SALTI
ID   BCSA_SALTI              Reviewed;         874 AA.
AC   Q8Z291;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE            EC=2.4.1.12;
GN   Name=bcsA; OrderedLocusNames=STY4181, t3898;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC       uridine 5'-diphosphate glucose to cellulose, which is produced as an
CC       extracellular component for mechanical and chemical protection at the
CC       onset of the stationary phase, when the cells exhibit multicellular
CC       behavior (rdar morphotype). Coexpression of cellulose and thin
CC       aggregative fimbriae leads to a hydrophobic network with tightly packed
CC       cells embedded in a highly inert matrix (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC         COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by bis-(3'-5') cyclic diguanylic acid
CC       (c-di-GMP). {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- DOMAIN: There are two conserved domains in the globular part of the
CC       protein: the N-terminal domain (domain A) contains the conserved DXD
CC       motif and is possibly involved in catalysis and substrate binding. The
CC       C-terminal domain (domain B) contains the QXXRW motif and is present
CC       only in processive glycosyl transferases. It could be involved in the
CC       processivity function of the enzyme, possibly required for holding the
CC       growing glycan chain in the active site.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD08006.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71373.1; -; Genomic_DNA.
DR   RefSeq; NP_458301.1; NC_003198.1.
DR   RefSeq; WP_001275344.1; NZ_WSUR01000001.1.
DR   AlphaFoldDB; Q8Z291; -.
DR   SMR; Q8Z291; -.
DR   STRING; 220341.16504990; -.
DR   EnsemblBacteria; AAO71373; AAO71373; t3898.
DR   KEGG; stt:t3898; -.
DR   KEGG; sty:STY4181; -.
DR   PATRIC; fig|220341.7.peg.4270; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_011907_5_0_6; -.
DR   OMA; QRLCYAN; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003919; Cell_synth_A.
DR   InterPro; IPR005150; Cellulose_synth.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR009875; PilZ_domain.
DR   Pfam; PF03552; Cellulose_synt; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF07238; PilZ; 1.
DR   PRINTS; PR01439; CELLSNTHASEA.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03030; CelA; 1.
PE   3: Inferred from homology;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..874
FT                   /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT                   /id="PRO_0000059269"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        547..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        592..612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        634..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        668..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        833..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          694..790
FT                   /note="PilZ"
FT   REGION          271..364
FT                   /note="Catalytic subdomain A"
FT   REGION          441..501
FT                   /note="Catalytic subdomain B"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   874 AA;  100021 MW;  3395D09CD0F51990 CRC64;
     MSALSRWLLI PPVSARLSER YQGYRRHGAS PFSAALGCLW TILAWIVFPL EHPRWQRIRD
     GHKALYPHIN AARPRPLDPA RYLIQTLWLV MISSTKERHE PRWRSFARLK DVRGRYHQWM
     DTLPERVRQK TTHLEKEKEL GHLSNGARRF ILGVIVTFSL ILALICITQP FNPLSQFIFL
     LLLWGVALLV RRMPGRFSAL MLIVLSLTVS CRYIWWRYTS TLNWDDPVSL VCGLILLFAE
     TYAWIVLVLG YFQVVWPLNR QPVPLPKEMS QWPTVDIFVP TYNEDLNVVK NTIYASLGID
     WPKDKLNIWI LDDGGRESFR QFARHVGVHY IARATHEHAK AGNINNALKH AKGEFVAIFD
     CDHVPTRSFL QMTMGWFLKE KQLAMMQTPH HFFSPDPFER NLGRFRKTPN EGTLFYGLVQ
     DGNDMWDATF FCGSCAVIRR KPLDEIGGIA VETVTEDAHT SLRLHRRGYT SAYMRIPQSA
     GLATESLSAH IGQRIRWARG MVQIFRLDNP LFGKGLKLAQ RLCYLNAMFH FLSGIPRLIF
     LTAPLAFLLL HAYIIYAPAL MIALFVIPHM VHASLTNSKI QGKYRHSFWS EIYETVLAWY
     IAPPTLVALI NPHKGKFNVT AKGGLVEEKY VDWVISRPYI FLVLLNLLGV AAGVWRYYYG
     PENETLTVIV SLVWVFYNLV ILGGAVAVSV ESKQVRRAHR VEIAMPGAIA REDGHLFSCT
     VHDFSDGGLG IKINGQAQVL EGQKVNLLLK RGQQEYVFPT QVVRVTGNEV GLQLMPLTTK
     QHIDFVQCTF ARADTWALWQ DSFPEDKPLE SLLDILKLGF RGYRHLAEFA PPSVKVIFRS
     LTALIAWIVS FIPRRPERQA AIQPSDRVMA QAQQ
 
 
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