BCSA3_KOMXY
ID BCSA3_KOMXY Reviewed; 745 AA.
AC Q9WX61;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cellulose synthase 1 catalytic subunit [UDP-forming];
DE EC=2.4.1.12;
GN Name=bcsAI;
OS Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=28448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 7664 / NBRC 13693;
RX PubMed=10382968; DOI=10.1093/dnares/6.2.109;
RA Umeda Y., Hirano A., Ishibashi M., Akiyama H., Onizuka T., Ikeuchi M.,
RA Inoue Y.;
RT "Cloning of cellulose synthase genes from Acetobacter xylinum JCM 7664:
RT implication of a novel set of cellulose synthase genes.";
RL DNA Res. 6:109-115(1999).
CC -!- FUNCTION: Catalytic subunit of cellulose synthase. It polymerizes
CC uridine 5'-diphosphate glucose to cellulose. The thick cellulosic mats
CC generated by this enzyme probably provide a specialized protective
CC environment to the bacterium (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 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; AB015802; BAA77585.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WX61; -.
DR SMR; Q9WX61; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
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 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..745
FT /note="Cellulose synthase 1 catalytic subunit [UDP-
FT forming]"
FT /id="PRO_0000059264"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
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 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 572..670
FT /note="PilZ"
FT REGION 147..240
FT /note="Catalytic subdomain A"
FT REGION 317..377
FT /note="Catalytic subdomain B"
FT REGION 708..745
FT /note="Disordered"
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 745 AA; 83519 MW; 57EA0457A226F815 CRC64;
MSEVQSSAPA ESWFGRFSNK ILSLRGASYV VGALGLCALL AATMVTLSLN EQMIVALVCV
AVFFIVGRRK SRRTQVFLEV LSALVSLRYL TWRLTETLDF DTWTQGILGV TLLLAELYAL
YMLFLSYFQT ISPLHRAPLP LPANPDEWPT VDIFIPTYDE ALSIVRLTVL GALGIDWPPD
KVNVYILDDG RREEFARFAE ACGARYIARP DNAHAKAGNL NYAIKHTTGD HILILDCDHI
PTRAFLQISM GWMVSDSNIA LLQTPHHFYS PDPFQRNLAV GYRTPPEGNL FYGVIQDGND
FWDATFFCGS CAILRRKAIE EIGGFATETV TEDAHTALRM QRKGWSTAYL RIPLASGLAT
ERLITHIGQR MRWARGMIQI FRVDNPMLGS GLKLGQRLCY LSAMTSFFFA IPRVIFLASP
LAFLFFSQNI IAASPLAVGV YAIPHMFHSI ATAAKVNKGW RYSFWSEVYE TVMALFLVRV
TIVTMLFPSK GKFNVTEKGG VLEREEFDLT ATYPNIIFAI IMALGLLRGL YALIFQHLDI
ISERAYALNC IWSVISLIIL MAVISVGRET KQLRQSHRIE AQIPVTVYDY DGNSSHGITE
DVSMGGVAIH LPWREVTPDH PVQVVIHAVL DGEEMNLPAT MIRSAQGKAV FTWSISNIQV
EAAVVRFVFG RADAWLQWNN YEDDRPLRSL WSLILSIKAL FRRKGQMIAH SRPKKKPIAL
PVERREPTTS QGGQKQEGKI SRAAS
