BCSA2_KOMSB
ID BCSA2_KOMSB Reviewed; 756 AA.
AC O82859;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE EC=2.4.1.12;
GN Name=bcsA;
OS Komagataeibacter sucrofermentans (strain ATCC 700178 / DSM 15973 / CECT
OS 7291 / JCM 9730 / LMG 18788 / BPR 2001) (Acetobacter xylinus subsp.
OS sucrofermentans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=1307942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700178 / DSM 15973 / CECT 7291 / JCM 9730 / LMG 18788 / BPR
RC 2001;
RX PubMed=9630539; DOI=10.1016/s0378-1119(98)00191-7;
RA Nakai T., Moriya A., Tonouchi N., Tsuchida T., Yoshinaga F., Horinouchi S.,
RA Sone Y., Mori H., Sakai F., Hayashi T.;
RT "Control of expression by the cellulose synthase (bcsA) promoter region
RT from Acetobacter xylinum BPR 2001.";
RL Gene 213:93-100(1998).
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).
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; AB010645; BAA31463.1; -; Genomic_DNA.
DR AlphaFoldDB; O82859; -.
DR SMR; O82859; -.
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..756
FT /note="Cellulose synthase catalytic subunit [UDP-forming]"
FT /id="PRO_0000059263"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 576..681
FT /note="PilZ"
FT REGION 147..242
FT /note="Catalytic subdomain A"
FT REGION 319..379
FT /note="Catalytic subdomain B"
FT REGION 721..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /evidence="ECO:0000255"
FT ACT_SITE 335
FT /evidence="ECO:0000255"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 756 AA; 84562 MW; 6954F39A25E73B0A CRC64;
MSEVQSPVPT ESRLGRISNK ILSLRGASYI VGALGLCALI AATTVTLNNN EQLIVAAVCV
VIFFVVGRGK SRRTQIFLEV LSALVSLRYL TWRLTETLDF NTWIQGILGV ILLMAELYAL
YMLFLSYFQT IQPLHRAPLP LPDNVDDWPT VDIFIPTYDE QLSIVRLTVL GALGIDWPPD
KVNVYILDDG VRPEFEQFAK DCGALYIGRV DVDSAHAKAG NLNHAIKRTS GDYILILDCD
HIPTRAFLQI AMGWMVADRK IALMQTPHHF YSPDPFQRNL AVGYRTPPEG NLFYGVIQDG
NDFWDATFFC GSCAILRREA IESIGGFAVE TVTEDAHTAL RMQRRGWSTA YLRIPVASGL
ATERLTTHIG QRMRWARGMI QIFRVDNPML GRGLKLGQRL CYLSAMTSFF FAIPRVIFLA
SPLAFLFAGQ NIIAAAPLAV AAYALPHMFH SIATAAKVNK GWRYSFWSEV YETTMALFLV
RVTIVTLLFP SKGKFNVTEK GGVLEEEEFD LGATYPNIIF ATIMMGGLLI GLFELIVRFN
QLDVIARNAY LLNCAWALIS LIILFAAIAV GRETKQVRYN HRVEAHIPVT VYDAPAEGQP
HTYYNATHGM TQDVSMGGVA VHIPLPDVTT GPVKKRIHAV LDGEEIDIPA TMLRCTNGKA
VFTWDNNDLD TERDIVRFVF GRADAWLQWN NYEDDRPLRS LWSLLLSIKA LFRKKGKIMA
NSRPKKKPLA LPVERREPTT IHSGQTQEGK ISRAAS
