ID WZA_ECOLI Reviewed; 379 AA.
AC P0A930; P71235; P71273; P76388; Q2MAY0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Putative polysaccharide export protein Wza;
DE Flags: Precursor;
GN Name=wza; OrderedLocusNames=b2062, JW2047;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8763957; DOI=10.1128/jb.178.14.4273-4280.1996;
RA Stout V.;
RT "Identification of the promoter region for the colanic acid polysaccharide
RT biosynthetic genes in Escherichia coli K-12.";
RL J. Bacteriol. 178:4273-4280(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-379.
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).
CC -!- FUNCTION: Probably involved in the export of the extracellular
CC polysaccharide colanic acid from the cell to medium.
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BexD/CtrA/VexA family. {ECO:0000305}.
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DR EMBL; U00096; AAC75123.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76576.1; -; Genomic_DNA.
DR EMBL; U52666; AAC44334.1; -; Genomic_DNA.
DR EMBL; U38473; AAC77833.1; -; Genomic_DNA.
DR PIR; E64972; E64972.
DR RefSeq; NP_416566.1; NC_000913.3.
DR RefSeq; WP_000978094.1; NZ_STEB01000002.1.
DR PDB; 7XFD; X-ray; 2.20 A; A/B=68-252.
DR PDB; 7XFF; X-ray; 2.30 A; A/B/C/D/E/F/G/H=68-252.
DR PDBsum; 7XFD; -.
DR PDBsum; 7XFF; -.
DR AlphaFoldDB; P0A930; -.
DR SMR; P0A930; -.
DR BioGRID; 4261254; 247.
DR DIP; DIP-11134N; -.
DR IntAct; P0A930; 2.
DR STRING; 511145.b2062; -.
DR TCDB; 1.B.18.3.1; the outer membrane auxiliary (oma) protein family.
DR PaxDb; 511145-b2062; -.
DR EnsemblBacteria; AAC75123; AAC75123; b2062.
DR GeneID; 75203925; -.
DR GeneID; 946558; -.
DR KEGG; ecj:JW2047; -.
DR KEGG; eco:b2062; -.
DR PATRIC; fig|1411691.4.peg.189; -.
DR EchoBASE; EB3336; -.
DR eggNOG; COG1596; Bacteria.
DR HOGENOM; CLU_038343_4_2_6; -.
DR InParanoid; P0A930; -.
DR OMA; GCTIIPG; -.
DR OrthoDB; 9808421at2; -.
DR PhylomeDB; P0A930; -.
DR BioCyc; EcoCyc:G7107-MONOMER; -.
DR BioCyc; MetaCyc:G7107-MONOMER; -.
DR UniPathway; UPA00631; -.
DR PRO; PR:P0A930; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015159; F:polysaccharide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0046377; P:colanic acid metabolic process; IGC:EcoCyc.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.70; -; 1.
DR Gene3D; 3.10.560.10; Outer membrane lipoprotein wza domain like; 2.
DR Gene3D; 3.30.1950.10; wza like domain; 1.
DR InterPro; IPR049712; Poly_export.
DR InterPro; IPR003715; Poly_export_N.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR InterPro; IPR040716; Wza_C.
DR PANTHER; PTHR33619; POLYSACCHARIDE EXPORT PROTEIN GFCE-RELATED; 1.
DR PANTHER; PTHR33619:SF5; POLYSACCHARIDE EXPORT PROTEIN GFCE-RELATED; 1.
DR Pfam; PF02563; Poly_export; 1.
DR Pfam; PF10531; SLBB; 1.
DR Pfam; PF18412; Wza_C; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Exopolysaccharide synthesis;
KW Ion transport; Lipoprotein; Membrane; Palmitate; Polysaccharide transport;
KW Porin; Reference proteome; Signal; Sugar transport; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..379
FT /note="Putative polysaccharide export protein Wza"
FT /id="PRO_0000025222"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 106
FT /note="P -> R (in Ref. 3; AAC44334 and 4; AAC77833)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="D -> G (in Ref. 4; AAC77833)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Q -> A (in Ref. 4; AAC77833)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="D -> G (in Ref. 4; AAC77833)"
FT /evidence="ECO:0000305"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:7XFF"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:7XFD"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7XFD"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:7XFD"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:7XFD"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:7XFD"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:7XFD"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:7XFD"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:7XFD"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:7XFD"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:7XFF"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:7XFD"
SQ SEQUENCE 379 AA; 41910 MW; C4902C8650B69B65 CRC64;
MMKSKMKLMP LLVSVTLISG CTVLPGSNMS TMGKDVIKQQ DADFDLDKMV NVYPLTPRLI
DQLRPRPNVA RPNMTLESEI ANYQYRVGPG DVLNVTVWDH PELTTPAGQY RSSSDTGNWV
QPDGTMFYPY IGKVHVVGKT LAEIRSDITG RLATYIADPQ VDVNIAAFRS QKAYISGQVN
KSGQQAITNV PLTILDAINA AGGLTDTADW RNVVLTHNGR EERISLQALM QNGDLNQNRL
LYPGDILYVP RNDDLKVFVM GEVKKQSTLK MDFSGMTLTE ALGNAEGIDM TTSNASGIFV
IRPLKGEGGR NGKIANIYQL DMSDATSLVM ATEFRLQPYD VVYVTTAPVS RWNRLINQLL
PTISGVRYMT DTASDIHNW
//
