ID   BCSA1_KOMXY             Reviewed;         754 AA.
AC   P19449;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE            EC=2.4.1.12;
GN   Name=bcsA;
OS   Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=28448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-42 AND
RP   196-206.
RC   STRAIN=1306-3;
RX   PubMed=2146681; DOI=10.1073/pnas.87.20.8130;
RA   Wong H.C., Fear A.L., Calhoon R.D., Eichinger G.H., Mayer R., Amikam D.,
RA   Benziman M., Gelfand D.H., Meade J.H., Emerick A.W., Bruner R.,
RA   Ben-Bassat A., Tal R.;
RT   "Genetic organization of the cellulose synthase operon in Acetobacter
RT   xylinum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8130-8134(1990).
RN   [2]
RP   ACTIVITY REGULATION.
RC   STRAIN=1306-3;
RX   PubMed=11297407; DOI=10.1021/bi0100236;
RA   Chang A.L., Tuckerman J.R., Gonzalez G., Mayer R., Weinhouse H., Volman G.,
RA   Amikam D., Benziman M., Gilles-Gonzalez M.-A.;
RT   "Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter
RT   xylinum, is a heme-based sensor.";
RL   Biochemistry 40:3420-3426(2001).
RN   [3]
RP   C-DI-GMP-BINDING.
RX   PubMed=16920715; DOI=10.1074/jbc.c600179200;
RA   Ryjenkov D.A., Simm R., Romling U., Gomelsky M.;
RT   "The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ
RT   domain protein YcgR controls motility in enterobacteria.";
RL   J. Biol. Chem. 281:30310-30314(2006).
CC   -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC       uridine 5'-diphosphate glucose to cellulose in a processive way. The
CC       thick cellulosic mats generated by this enzyme probably provide a
CC       specialized protective environment to the bacterium. Binds c-di-GMP
CC       with a dissociation constant of 30 uM.
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;
CC   -!- ACTIVITY REGULATION: Activated by bis-(3'-5') cyclic diguanylic acid
CC       (c-di-GMP). {ECO:0000269|PubMed:11297407}.
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Cellulose is produced at a linear rate with respect to cell
CC       growth when O(2) is present.
CC   -!- DOMAIN: There are two conserved domains in the globular part of the
CC       catalytic subunit: the N-terminal domain (domain A) contains the
CC       conserved DXD motif and is possibly involved in catalysis and substrate
CC       binding. The C-terminal domain (domain B) contains the QXXRW motif and
CC       is present only in processive glycosyl transferases. It could be
CC       involved in the processivity function of the enzyme, possibly required
CC       for holding the growing glycan chain in the active site.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; M37202; AAA21884.1; -; Genomic_DNA.
DR   PIR; A43735; A43735.
DR   AlphaFoldDB; P19449; -.
DR   SMR; P19449; -.
DR   STRING; 1220579.GCA_001571345_00314; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   BRENDA; 2.4.1.12; 50.
DR   UniPathway; UPA00694; -.
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   1: Evidence at protein level;
KW   c-di-GMP; Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Direct protein sequencing; Glycosyltransferase; Membrane;
KW   Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..754
FT                   /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT                   /id="PRO_0000059262"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        549..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          574..679
FT                   /note="PilZ"
FT   REGION          147..240
FT                   /note="Catalytic subdomain A"
FT   REGION          317..377
FT                   /note="Catalytic subdomain B"
FT   REGION          717..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000255"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   754 AA;  84443 MW;  8D5FC1FE62E2C068 CRC64;
     MSEVQSPVPA ESRLDRFSNK ILSLRGANYI VGALGLCALI AATTVTLSIN EQLIVALVCV
     LVFFIVGRGK SRRTQIFLEV LSALVSLRYL TWRLTETLDF DTWIQGGLGV TLLMAELYAL
     YMLFLSYFQT IQPLHRAPLP LPDNVDDWPT VDIFIPTYDE QLSIVRLTVL GALGIDWPPD
     KVNVYILDDG VRPEFEQFAK DCGALYIGRV DSSHAKAGNL NHAIKRTSGD YILILDCDHI
     PTRAFLQIAM GWMVADRKIA LMQTPHHFYS PDPFQRNLAV GYRTPPEGNL FYGVIQDGND
     FWDATFFCGS CAILRREAIE SIGGFAVETV TEDAHTALRM QRRGWSTAYL RIPVASGLAT
     ERLTTHIGQR MRWARGMIQI FRVDNPMLGG GLKLGQRLCY LSAMTSFFFA IPRVIFLASP
     LAFLFFGQNI IAASPLAVLA YAIPHMFHSI ATAAKVNKGW RYSFWSEVYE TTMALFLVRV
     TIITLMFPSK GKFNVTEKGG VLEEEEFDLG ATYPNIIFAG IMTLGLLIGL FELTFHFNQL
     AGIAKRAYLL NCIWAMISLI ILLAAIAVGR ETKQVRYNHR VEAHIPVTVY EAPVAGQPNT
     YHNATPGMTQ DVSMGGVAVH MPWPDVSTGP VKTRIHAVLD GEEIDIPATM LRCKNGKAVF
     TWDNNDLDTE RDIVRFVFGR ADAWLQWNNY EDDRPLRSLW SLLLSIKALF RKKGKMMANS
     RPKRKPLALP VERREPTTIQ SGQTQEGKIS RAAS