WZXE_ECOLI
ID WZXE_ECOLI Reviewed; 416 AA.
AC P0AAA7; P27834; Q2M8A0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lipid III flippase {ECO:0000255|HAMAP-Rule:MF_02024, ECO:0000305};
GN Name=wzxE {ECO:0000255|HAMAP-Rule:MF_02024, ECO:0000303|PubMed:12621029};
GN Synonyms=wzx, yifJ; OrderedLocusNames=b3792, JW3766;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
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 [3]
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 [4]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=12621029; DOI=10.1074/jbc.m301750200;
RA Rick P.D., Barr K., Sankaran K., Kajimura J., Rush J.S., Waechter C.J.;
RT "Evidence that the wzxE gene of Escherichia coli K-12 encodes a protein
RT involved in the transbilayer movement of a trisaccharide-lipid intermediate
RT in the assembly of enterobacterial common antigen.";
RL J. Biol. Chem. 278:16534-16542(2003).
RN [5]
RP FUNCTION, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=16199561; DOI=10.1128/jb.187.20.6917-6927.2005;
RA Kajimura J., Rahman A., Rick P.D.;
RT "Assembly of cyclic enterobacterial common antigen in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 187:6917-6927(2005).
RN [6]
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 [7]
RP SUBUNIT.
RX PubMed=16816184; DOI=10.1128/jb.00461-06;
RA Marolda C.L., Tatar L.D., Alaimo C., Aebi M., Valvano M.A.;
RT "Interplay of the Wzx translocase and the corresponding polymerase and
RT chain length regulator proteins in the translocation and periplasmic
RT assembly of lipopolysaccharide o antigen.";
RL J. Bacteriol. 188:5124-5135(2006).
CC -!- FUNCTION: Mediates the transbilayer movement of Und-PP-GlcNAc-ManNAcA-
CC Fuc4NAc (lipid III) from the inner to the outer leaflet of the
CC cytoplasmic membrane during the assembly of enterobacterial common
CC antigen (ECA). Required for the assembly of the phosphoglyceride-linked
CC form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA
CC (ECA(CYC)). Could also mediate the translocation of Und-PP-GlcNAc.
CC {ECO:0000269|PubMed:12621029, ECO:0000269|PubMed:16199561}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02024,
CC ECO:0000269|PubMed:12621029, ECO:0000269|PubMed:16199561}.
CC -!- SUBUNIT: Probably part of a complex composed of WzxE, WzyE and WzzE.
CC {ECO:0000255|HAMAP-Rule:MF_02024, ECO:0000305|PubMed:16816184}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02024, ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02024}.
CC -!- DISRUPTION PHENOTYPE: Null mutation results in the accumulation of
CC lipid III and cell death. {ECO:0000269|PubMed:12621029}.
CC -!- SIMILARITY: Belongs to the polysaccharide transport (PST) (TC 2.A.66.2)
CC family. {ECO:0000255|HAMAP-Rule:MF_02024, ECO:0000305}.
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DR EMBL; M87049; AAA67592.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76797.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77506.1; -; Genomic_DNA.
DR PIR; C65183; C65183.
DR RefSeq; NP_418239.1; NC_000913.3.
DR RefSeq; WP_000050265.1; NZ_STEB01000021.1.
DR AlphaFoldDB; P0AAA7; -.
DR SMR; P0AAA7; -.
DR BioGRID; 4262107; 228.
DR STRING; 511145.b3792; -.
DR TCDB; 2.A.66.2.3; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; P0AAA7; -.
DR PRIDE; P0AAA7; -.
DR EnsemblBacteria; AAC76797; AAC76797; b3792.
DR EnsemblBacteria; BAE77506; BAE77506; BAE77506.
DR GeneID; 58389391; -.
DR GeneID; 948294; -.
DR KEGG; ecj:JW3766; -.
DR KEGG; eco:b3792; -.
DR PATRIC; fig|1411691.4.peg.2914; -.
DR EchoBASE; EB1449; -.
DR eggNOG; COG2244; Bacteria.
DR HOGENOM; CLU_042154_0_0_6; -.
DR InParanoid; P0AAA7; -.
DR OMA; KFTIMAL; -.
DR PhylomeDB; P0AAA7; -.
DR BioCyc; EcoCyc:EG11486-MON; -.
DR BioCyc; MetaCyc:EG11486-MON; -.
DR UniPathway; UPA00566; -.
DR PRO; PR:P0AAA7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0140303; F:intramembrane lipid transporter activity; IDA:EcoCyc.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IMP:EcoCyc.
DR CDD; cd13125; MATE_like_10; 1.
DR HAMAP; MF_02024; WzxE; 1.
DR InterPro; IPR002797; Polysacc_synth.
DR InterPro; IPR044550; WzxE.
DR InterPro; IPR032896; WzxE_Proteobacteria.
DR Pfam; PF01943; Polysacc_synt; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..416
FT /note="Lipid III flippase"
FT /id="PRO_0000065989"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 39..45
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 67..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 106..121
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 143..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 166..174
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 196..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 238..259
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 281..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 324..334
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 356..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02024"
FT TOPO_DOM 413..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 416 AA; 44960 MW; 001690A4E86CADF5 CRC64;
MSLAKASLWT AASTLVKIGA GLLVGKLLAV SFGPAGLGLA ANFRQLITVL GVLAGAGIFN
GVTKYVAQYH DNPQQLRRVV GTSSAMVLGF STLMALVFVL AAAPISQGLF GNTDYQGLVR
LVALVQMGIA WGNLLLALMK GFRDAAGNAL SLIVGSLIGV LAYYVSYRLG GYEGALLGLA
LIPALVVIPA AIMLIKRGVI PLSYLKPSWD NGLAGQLSKF TLMALITSVT LPVAYIMMRK
LLAAQYSWDE VGIWQGVSSI SDAYLQFITA SFSVYLLPTL SRLTEKRDIT REVVKSLKFV
LPAVAAASFT VWLLRDFAIW LLLSNKFTAM RDLFAWQLVG DVLKVGAYVF GYLVIAKASL
RFYILAEVSQ FTLLMVFAHW LIPAHGALGA AQAYMATYIV YFSLCCGVFL LWRRRA
