WCAJ_ECOLI
ID WCAJ_ECOLI Reviewed; 464 AA.
AC P71241; P76381;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase;
DE Short=UDP-Glc:Und-P Glc-1-P transferase;
DE EC=2.7.8.31;
DE AltName: Full=Colanic acid biosynthesis UDP-glucose lipid carrier transferase;
DE AltName: Full=Glucosyl-P-P-undecaprenol synthase;
GN Name=wcaJ; OrderedLocusNames=b2047, JW2032;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8759852; DOI=10.1128/jb.178.16.4885-4893.1996;
RA Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.;
RT "Organization of the Escherichia coli K-12 gene cluster responsible for
RT production of the extracellular polysaccharide colanic acid.";
RL J. Bacteriol. 178:4885-4893(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ROLE IN COLANIC ACID BIOSYNTHESIS, PATHWAY,
RP SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=22408159; DOI=10.1128/jb.06052-11;
RA Patel K.B., Toh E., Fernandez X.B., Hanuszkiewicz A., Hardy G.G.,
RA Brun Y.V., Bernards M.A., Valvano M.A.;
RT "Functional characterization of UDP-glucose:undecaprenyl-phosphate glucose-
RT 1-phosphate transferases of Escherichia coli and Caulobacter crescentus.";
RL J. Bacteriol. 194:2646-2657(2012).
CC -!- FUNCTION: Is the initiating enzyme for colanic acid (CA) synthesis.
CC Catalyzes the transfer of the glucose-1-phosphate moiety from UDP-Glc
CC onto the carrier lipid undecaprenyl phosphate (C55-P), forming a
CC phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-undecaprenol
CC (Glc-PP-C55). Also possesses a weak galactose-1-P transferase activity.
CC {ECO:0000269|PubMed:22408159}.
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 Evidence={ECO:0000269|PubMed:22408159};
CC -!- PATHWAY: Exopolysaccharide biosynthesis; colanic acid biosynthesis.
CC {ECO:0000269|PubMed:22408159}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22408159}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22408159}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a non-mucoid
CC phenotype. {ECO:0000269|PubMed:22408159}.
CC -!- MISCELLANEOUS: Complements holdfast synthesis in the C.crescentus
CC mutant lacking hfsE, pssY and pssZ genes. Can also partially complement
CC the O-antigen defect in the S.typhimurium wbaP deletion strain
CC (PubMed:22408159). {ECO:0000305|PubMed:22408159}.
CC -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC {ECO:0000305}.
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DR EMBL; U38473; AAC77848.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75108.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15900.1; -; Genomic_DNA.
DR PIR; F64970; F64970.
DR RefSeq; NP_416551.1; NC_000913.3.
DR RefSeq; WP_000183107.1; NZ_LN832404.1.
DR AlphaFoldDB; P71241; -.
DR SMR; P71241; -.
DR BioGRID; 4263311; 198.
DR DIP; DIP-11125N; -.
DR IntAct; P71241; 1.
DR STRING; 511145.b2047; -.
DR PaxDb; P71241; -.
DR PRIDE; P71241; -.
DR EnsemblBacteria; AAC75108; AAC75108; b2047.
DR EnsemblBacteria; BAA15900; BAA15900; BAA15900.
DR GeneID; 946583; -.
DR KEGG; ecj:JW2032; -.
DR KEGG; eco:b2047; -.
DR PATRIC; fig|1411691.4.peg.204; -.
DR EchoBASE; EB3345; -.
DR eggNOG; COG2148; Bacteria.
DR HOGENOM; CLU_024920_0_1_6; -.
DR InParanoid; P71241; -.
DR OMA; NWSVLFD; -.
DR PhylomeDB; P71241; -.
DR BioCyc; EcoCyc:G7098-MON; -.
DR BioCyc; MetaCyc:G7098-MON; -.
DR UniPathway; UPA00980; -.
DR PRO; PR:P71241; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IBA:GO_Central.
DR GO; GO:0089702; F:undecaprenyl-phosphate glucose phosphotransferase activity; IDA:EcoCyc.
DR GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR003362; Bact_transf.
DR InterPro; IPR017475; EPS_sugar_tfrase.
DR InterPro; IPR017473; Undecaprenyl-P_gluc_Ptfrase.
DR Pfam; PF02397; Bac_transf; 1.
DR TIGRFAMs; TIGR03025; EPS_sugtrans; 1.
DR TIGRFAMs; TIGR03023; WcaJ_sugtrans; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Exopolysaccharide synthesis;
KW Glycosyltransferase; Lipopolysaccharide biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="UDP-glucose:undecaprenyl-phosphate glucose-1-
FT phosphate transferase"
FT /id="PRO_0000166470"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..38
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..464
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 202..203
FT /note="AG -> RA (in Ref. 1; AAC77848)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> P (in Ref. 1; AAC77848)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="Q -> K (in Ref. 1; AAC77848)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="ML -> IV (in Ref. 1; AAC77848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 52408 MW; 0103B570EE51EBDB CRC64;
MTNLKKRERA KTNASLISMV QRFSDITIMF AGLWLVCEVS GLSFLYMHLL VALITLVVFQ
MLGGITDFYR SWRGVRAATE FALLLQNWTL SVIFSAGLVA FNNDFDTQLK IWLAWYALTS
IGLVVCRSCI RIGAGWLRNH GYNKRMVAVA GDLAAGQMLM ESFRNQPWLG FEVVGVYHDP
KPGGVSNDWA GNLQQLVEDA KAGKIHNVYI AMQMCDGARV KKLVHQLADT TCSVLLIPDV
FTFNILHSRL EEMNGVPVVP LYDTPLSGVN RLLKRAEDIV LATLILLLIS PVLCCIALAV
KLSSPGPVIF RQTRYGMDGK PIKVWKFRSM KVMENDKVVT QATQNDPRVT KVGNFLRRTS
LDELPQFINV LTGGMSIVGP RPHAVAHNEQ YRQLIEGYML RHKVKPGITG WAQINGWRGE
TDTLEKMEKR VEFDLEYIRE WSVWFDIKIV FLTVFKGFVN KAAY
