ID   BCSY_KOMXY              Reviewed;         386 AA.
AC   Q9WX70;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Putative membrane-bound transacylase BcsY;
DE            EC=2.3.-.-;
GN   Name=bcsY;
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: May acylate a glucose moiety into cellulose fibrils, in
CC       cooperation with BcsABII and BcsCII.
CC   -!- PATHWAY: Glycan metabolism; bacterial cellulose biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; AB015803; BAA77595.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WX70; -.
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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Cellulose biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..386
FT                   /note="Putative membrane-bound transacylase BcsY"
FT                   /id="PRO_0000208069"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   386 AA;  42859 MW;  AEB5300BCEB74B94 CRC64;
     MLQLNPTPPA PGRWRTILEN DFFPKNRRRD IDGLRGLAIA LVVLFHAGWL KGGFIGVDVF
     VVISGYFMGR SALMQHPFQP VRFVCRRLYR LLPALLCMVA LVSAGMLWWV LQSDRADIAL
     NGAYALVYLS NIWASGHVGY FQGQAVAYPF LHTWSLSLEM QFYAIIFIMA LLLPLTRHRR
     LVLSAIFSAS AAYCAYAWHT GDSQAYYNIL DRLWQFALGT MVWMLPRPKL PRAAADAVYA
     AAVAVIVGAG LFYPLSYACP SWMTVFPCGA VVLIIMLPDT RVGRWCLVPL SPLGVISYSV
     YLWHWPGIVV ANYLLFFQVH GAMMAGVLAL VMVVSLLSYV LVERTGLDYE NRAPVAARNR
     GAALLVAACL GLAAVLAYIS HVSRVH