ID   BCSA5_KOMXY             Reviewed;        1518 AA.
AC   Q9WX75;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Putative cellulose synthase 3;
DE   Includes:
DE     RecName: Full=Cellulose synthase catalytic subunit [UDP-forming];
DE              EC=2.4.1.12;
DE   Includes:
DE     RecName: Full=Cyclic di-GMP-binding domain;
DE     AltName: Full=Cellulose synthase 3 regulatory subunit;
GN   Name=bcsABII-B;
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   -!- 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   -!- 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: In the N-terminal section; belongs to the
CC       glycosyltransferase 2 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the AcsB/BcsB family.
CC       {ECO:0000305}.
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DR   EMBL; AB015804; BAA77600.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WX75; -.
DR   SMR; Q9WX75; -.
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; IPR003920; Cell_synth_B.
DR   InterPro; IPR018513; Cell_synthase_bac.
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; PF03170; BcsB; 1.
DR   Pfam; PF03552; Cellulose_synt; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF07238; PilZ; 1.
DR   PRINTS; PR01440; CELLSNTHASEB.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03030; CelA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cellulose biosynthesis;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1518
FT                   /note="Putative cellulose synthase 3"
FT                   /id="PRO_0000059266"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1481..1501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          569..668
FT                   /note="PilZ"
FT   REGION          1..731
FT                   /note="Catalytic"
FT   REGION          144..237
FT                   /note="Catalytic subdomain A"
FT   REGION          314..374
FT                   /note="Catalytic subdomain B"
FT   REGION          732..1518
FT                   /note="Cyclic di-GMP binding domain"
FT                   /evidence="ECO:0000250"
FT   REGION          765..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000255"
FT   SITE            233
FT                   /note="Important for substrate binding"
FT                   /evidence="ECO:0000255"
FT   SITE            235
FT                   /note="Important for substrate binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1518 AA;  166465 MW;  7D7634503183DAB6 CRC64;
     MYGTWFTTGK VTDLLARTGL DRVPVWVPVV LGVVLMAFVG SVRIDPALQG WVSIGTVTLL
     LVLNRRRGRG ITVFLMMLSL LVSLRYIVWR LTATVQFSNW LQTALAVLLL LAEAYALMTL
     CLSYFQMAWP LRRREHPLPE DMAQWPSVDV FVPSYNEELS LVRSTVLGAL DLDWPADRLN
     VYILDDGRRK AFHDFAVEAG AGYIIRAENN HAKAGNLNHA LAVTDSPFAV IFDCDHVPTR
     GFLRRTIGWM MADPNLALLQ TPHHFYAPDP FQRNLAGGMH VPPEGNMFYG LVQDGNDFWD
     ATFFCGSCAI IRREAVMGIG GFATETVTED AHTALKMQRR GWGTAYLREP LAAGLATERL
     ILHIGQRVRW ARGMIQIMRL DNPMLGAGLR WEQRLCYLSA MSHFLFAIPR LTFLVSPLAF
     LFLGQNIIAA SPLAISVYAL PHIFHSVITL SRIEGRWRYS FWSEIYETSL ALFLVRITIV
     TLLQPHKGKF NVTDKGGLLA RGYFDWDAVY PNVILAGVLC AALLRGVFGI VWQFHDRLAL
     QSFILNTLWV VISLIIVLAS IAVGRETRQT RNAPRVSVRL PVVVTDAHGR QMEGHTHDIS
     LGGLAVGTRL ATPDMVGGEV TVRYDSARDG IHVGVPARVL DARDGTLRLR WAVRDLEDER
     QVVSMVFGRN DAWAGWADFA PDRPLRSLAM VFRSIGGLLR RRPAEAPRAL HEMGEGELPA
     TEEKLEKQSF VLKPVPRSAR HGATASAALF VAFTALVPAA MAQEAPSPDQ SGVTAETPFG
     DSNTGVVPDA LPAIDPAVAD RISDAEVTRT LTFRNLGATT GPLTLRGYSP LQGLDVVVPA
     NRVVTHAQLT LSGALSPSLL PEANAVTVTL NEQYVGTLKV DPQHPQFGPV SFDIDPLYFT
     GDNKLNFHFA GEYRRDCNDL FNEILWARIS DMSRITLTTV RITPERKLSR LPAPFFDPNQ
     RSTLRVPVVL PATGDRGALR AAGLVASWFG RIADFRKLSF PVSTTIPASG NAVEVGVNLP
     VDAEGGRPAG PMLAEVANPN DRWGTVLVVT GRTAQEVEVA ARALVFSPDT LGGVASKVVS
     DVSLETRHPY DAPAFVPTDR PVRFGELVGA ADLQGGGFAP AGMTLPFHLP PDLYTWRGRP
     FLMNMWVRAP GGPVVDLETS RVDVSLNNNY LQSYTLSPPG LWRKWSERLV NQHAGAVGHV
     TALPPWLLFG QNQLQFNFDA RPIDRGACRR TPGDIHMSVD SDSTLDFRRG YHFAEMPNLS
     YFAEAAFPFS RMADLSETTV VLPDHPDTGT TGAFLDLMGF FGASTWYPAA GVTVMGADEV
     AQTPPKGDIV VLGTAAQLGG AASGLLARSP YVIHDRHITV GQRMGLQGIW YLFQDHDHAG
     LKDGVTANLN APIAEAGVLL AAQSPYDSQR SVVAFTGDTP ERIHDLVLSL RNKGDLPSLQ
     GDLVLKNGDR FTSYRTAPVY TVGSLPLWLR LDWFLGHHPS ALYLAGLAGA GLAALGVWAW
     LRGWSRRRIA RDDLTGEL