BCSA_SALTY
ID BCSA_SALTY Reviewed; 874 AA.
AC Q93IN2;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE EC=2.4.1.12;
GN Name=bcsA; OrderedLocusNames=STM3619;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=11260463; DOI=10.1046/j.1365-2958.2001.02337.x;
RA Zogaj X., Nimtz M., Rohde M., Bokranz W., Roemling U.;
RT "The multicellular morphotypes of Salmonella typhimurium and Escherichia
RT coli produce cellulose as the second component of the extracellular
RT matrix.";
RL Mol. Microbiol. 39:1452-1463(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=11929533; DOI=10.1046/j.1365-2958.2002.02802.x;
RA Solano C., Garcia B., Valle J., Berasain C., Ghigo J.-M., Gamazo C.,
RA Lasa I.;
RT "Genetic analysis of Salmonella enteritidis biofilm formation: critical
RT role of cellulose.";
RL Mol. Microbiol. 43:793-808(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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.
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; AJ315770; CAC44015.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22479.1; -; Genomic_DNA.
DR EMBL; AJ315148; CAC86199.1; -; Genomic_DNA.
DR RefSeq; NP_462520.1; NC_003197.2.
DR RefSeq; WP_001275340.1; NC_003197.2.
DR AlphaFoldDB; Q93IN2; -.
DR SMR; Q93IN2; -.
DR STRING; 99287.STM3619; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q93IN2; -.
DR EnsemblBacteria; AAL22479; AAL22479; STM3619.
DR GeneID; 1255142; -.
DR KEGG; stm:STM3619; -.
DR PATRIC; fig|99287.12.peg.3825; -.
DR HOGENOM; CLU_011907_5_0_6; -.
DR OMA; QRLCYAN; -.
DR PhylomeDB; Q93IN2; -.
DR BioCyc; SENT99287:STM3619-MON; -.
DR UniPathway; UPA00694; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0016758; F:hexosyltransferase activity; IBA:GO_Central.
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; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009875; PilZ_domain.
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; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..874
FT /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT /id="PRO_0000059270"
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; 100044 MW; 4C9421B58606310A 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 HFARHVGVHY IARTTHEHAK AGNINNALKH AKGEFVAIFD
CDHVPTRSFL QMTMGWFLKE KQLAMMQTPH HFFSPDPFER NLGRFRKTPN EGTLFYGLVQ
DGNDMWDATF FCGSCAVIRR KPLDEIGGIA VETVTEDAHT SLRLHRRGYT SAYMRIPQAA
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
