ACEA_KOMXY
ID ACEA_KOMXY Reviewed; 532 AA.
AC Q44576;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Undecaprenyl-phosphate glucose phosphotransferase;
DE EC=2.7.8.31;
GN Name=aceA;
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=C1;
RX PubMed=8935665; DOI=10.1111/j.1574-6968.1996.tb08092.x;
RA Griffin A.M., Morris V.J., Gasson M.J.;
RT "Identification, cloning and sequencing the aceA gene involved in acetan
RT biosynthesis in Acetobacter xylinum.";
RL FEMS Microbiol. Lett. 137:115-121(1996).
RN [2]
RP FUNCTION.
RX PubMed=12353627; DOI=10.1271/bbb.66.1677;
RA Ishida T., Sugano Y., Nakai T., Shoda M.;
RT "Effects of acetan on production of bacterial cellulose by Acetobacter
RT xylinum.";
RL Biosci. Biotechnol. Biochem. 66:1677-1681(2002).
CC -!- FUNCTION: Involved in the biosynthesis of the exopolysaccharide acetan,
CC a water-soluble polysaccharide involved in production of bacterial
CC cellulose (BC). {ECO:0000269|PubMed:12353627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-alpha-D-glucose
CC = alpha-D-glucosyl di-trans,octa-cis-undecaprenyl diphosphate + UMP;
CC Xref=Rhea:RHEA:28126, ChEBI:CHEBI:57865, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:60392, ChEBI:CHEBI:61254; EC=2.7.8.31;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC {ECO:0000305}.
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DR EMBL; X93149; CAA63648.1; -; Genomic_DNA.
DR PIR; T44788; T44788.
DR AlphaFoldDB; Q44576; -.
DR SMR; Q44576; -.
DR PRIDE; Q44576; -.
DR BioCyc; MetaCyc:MON-15987; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR003362; Bact_transf.
DR InterPro; IPR017475; EPS_sugar_tfrase.
DR Pfam; PF02397; Bac_transf; 1.
DR TIGRFAMs; TIGR03025; EPS_sugtrans; 1.
PE 3: Inferred from homology;
KW Exopolysaccharide synthesis; Glycosyltransferase; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Undecaprenyl-phosphate glucose phosphotransferase"
FT /id="PRO_0000424202"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 60276 MW; E29B672C9F956A64 CRC64;
MGIISHSIVQ CGKWQAGPAR RQVVFRVHRR CFKMSEALRH LKNGETDLSS LPSGLDSIPR
RIHTARGVDD SFSYRHPVLP QVVVLSDAFC VCLAVVACIA WQRIYDTPDE LSGALLLANI
MAAGAFFLFP KNVPLLDIPD ITKVSVQIRY LLPPVAFGEV VFCTVLVMLS WPFGVTVRMG
MEWLTFVVAI LFVERCVGTY ILHTPTMTRR LARKVAIIGS GSEATQMATR INTRMQRMFR
LVGTFDDQGG DSDGTVEELV LRAREDHIDA VIICFPPACG QQHVMDVLWR LRGVLADVYV
VPSLMTEDCH GWPVERFGPF SLTVLQRRPL SEWDMLEKRA FDLTASVLLL LALAPLLTLV
ALAIKLDSRG PVLFCQPRQG FNNRYFNVFK FRSMYTDMSD LDAARQTSRT DPRVTRIGRW
IRRLSIDELP QLFNVLRGEM SLVGPRPHAP QTRAGGQLLH EAMEEYVARH RVQPGITGWA
QINGSRGELV TRDDLCRRVV LDLEYIRAWS IWLDIKIIFL TIKREIFSRN AF