ID   BCSA_XANAC              Reviewed;         729 AA.
AC   P58932;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE            EC=2.4.1.12;
GN   Name=bcsA; OrderedLocusNames=XAC3518;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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 (By
CC       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; AE008923; AAM38361.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58932; -.
DR   SMR; P58932; -.
DR   STRING; 190486.XAC3518; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; AAM38361; AAM38361; XAC3518.
DR   KEGG; xac:XAC3518; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_011907_5_0_6; -.
DR   OMA; YSFWGEI; -.
DR   UniPathway; UPA00694; -.
DR   Proteomes; UP000000576; 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..729
FT                   /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT                   /id="PRO_0000059272"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        549..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        610..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          575..671
FT                   /note="PilZ"
FT   REGION          151..244
FT                   /note="Catalytic subdomain A"
FT   REGION          321..381
FT                   /note="Catalytic subdomain B"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000255"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   729 AA;  80915 MW;  B9C08BB995E795B1 CRC64;
     MPLVVPHAAM PEGRLMTAAS RRSASPLPTL ATWALWLLGA LLLVFVVAVP MDVTQQLVFS
     GVLFAVALAV RNRGGRVVIL MMMGMSLAVS CRYIWWRMTQ TMGVGSAVDF ILGLGLLGAE
     LYAFVILVLG YFQVLWPLNR KPVPLPADQR LWPSVDVFIP TYNEPLSVVR TTVLAASVID
     WPAGKITIHL LDDGRRDEFR AFCAEVGINY VTRTNNAHAK AGNINAALKK CSGDYVAIFD
     CDHIPTRSFL QVAMGWFLHD TKLALVQMPH YFFSPDPFER NLDTHGKVPN EGELFYGLLQ
     DGNDQWNATF FCGSCAVIKR TALEEVGGVA VETVTEDAHT ALKLQRRGYR TAYLAVPQAA
     GLATESLSGH VAQRIRWARG MAQIARIDNP LLGRGLKLSQ RLCYLNAMLH FFYGVPRIIY
     LTAPLAYLFF GAHVIQASAL MILAYALPHI LQANLTNLRV QSRFRHLLWN EVYETTLAWY
     IFRPTLVALL NPKLGKFNVT PKGGLVARSY FDAQIAKPYL FLLLLNVVGM VAGVLRLIYV
     GGSGEQQTIW FNLAWTLYNM VLLGATIATA SETRQVRSAH RVPLDVPVTL YLPDGDVLPS
     RSVNFSTGGM AIMLAQPQPI EPGLPVQIGL SHRGVEQTLP AVVRQDRDGQ VSIQFTQMSM
     EQERWLVAST FARADIWLSQ WGQHDRDAFW RSMGQVLEAS ARGFGRLGGH IVDSARQGFR
     PRRAVDLES