ID   EPTA_HELPY              Reviewed;         521 AA.
AC   O24867; Q1PDD3;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Phosphoethanolamine transferase EptA {ECO:0000305};
DE            EC=2.7.-.- {ECO:0000305};
DE   AltName: Full=Lipid A 1-phosphoethanolamine transferase {ECO:0000303|PubMed:15489235};
GN   Name=eptA {ECO:0000303|PubMed:15489235};
GN   OrderedLocusNames=HP_0022, C694_00105;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, SUBSTRATE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND STRUCTURE OF LIPID A.
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=15489235; DOI=10.1074/jbc.m406480200;
RA   Tran A.X., Karbarz M.J., Wang X., Raetz C.R., McGrath S.C., Cotter R.J.,
RA   Trent M.S.;
RT   "Periplasmic cleavage and modification of the 1-phosphate group of
RT   Helicobacter pylori lipid A.";
RL   J. Biol. Chem. 279:55780-55791(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RA   Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA   Kostrjukova E., Govorun V.;
RT   "Draft genome of Helicobacter pylori.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably catalyzes the addition of a phosphoethanolamine
CC       moiety to the dephosphorylated 1-position of the disaccharide backbone
CC       of lipid A. Lipid A that is 1-phosphorylated is not a substrate for
CC       this enzyme. {ECO:0000269|PubMed:15489235}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000305|PubMed:15489235}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P36555}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P36555}.
CC   -!- MISCELLANEOUS: In this organism most lipid A is tetraacylated without a
CC       phosphate group at the 4'-position and has a phosphoethanolamine
CC       residue at the 1-position. {ECO:0000269|PubMed:15489235}.
CC   -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ447325; ABE02822.1; -; Genomic_DNA.
DR   EMBL; AE000511; AAD07089.1; -; Genomic_DNA.
DR   EMBL; CP003904; AFV41242.1; -; Genomic_DNA.
DR   PIR; F64522; F64522.
DR   RefSeq; NP_206824.1; NC_000915.1.
DR   RefSeq; WP_000157542.1; NC_018939.1.
DR   AlphaFoldDB; O24867; -.
DR   SMR; O24867; -.
DR   STRING; 85962.C694_00105; -.
DR   PaxDb; O24867; -.
DR   EnsemblBacteria; AAD07089; AAD07089; HP_0022.
DR   KEGG; heo:C694_00105; -.
DR   KEGG; hpy:HP_0022; -.
DR   PATRIC; fig|85962.47.peg.21; -.
DR   eggNOG; COG2194; Bacteria.
DR   HOGENOM; CLU_018534_1_1_7; -.
DR   OMA; NSIAFYF; -.
DR   PhylomeDB; O24867; -.
DR   BioCyc; MetaCyc:HP_RS00130-MON; -.
DR   BRENDA; 2.7.8.43; 2604.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR   GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IBA:GO_Central.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR012549; EptA-like_N.
DR   InterPro; IPR040423; PEA_transferase.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR30443; PTHR30443; 1.
DR   Pfam; PF08019; EptA_B_N; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..521
FT                   /note="Phosphoethanolamine transferase EptA"
FT                   /id="PRO_0000432500"
FT   TRANSMEM        18..38
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   521 AA;  58859 MW;  96C20817A166FD79 CRC64;
     MASLFHLRFL KPLSCLQAGL LYSLIFGVLY HFPLFVYVYK ESNQVSFIAM MVVVLFCVNG
     ALFLALGLIS ASLMRWSAIV FSLLNSVAFY FISAYKVFLN KSMMGNVLNT NTHEVLGFLS
     VKLFVFIVVF GVLPGYVIYK IPLKNSSKKA PFLAILALVF IFIASALANT KNWLWFDKHA
     KFIGGLILPF AYSVNAFRVS ALKFFAPTIK PLPLFSPNHS HSFVVLVIGE SARKHNYALY
     GYQKPTTPRL SKRLADNELT LFNATSCATY TTASLECILD SSFKNNAYEN LPTYLTKAGI
     KVFWYSANDG EKNVKVTSYL KNYELIQKCP NCEAIAPYDE SLLYNLPDLL KEHSNENVLL
     ILHLAGSHGP NYDNKVPLNF RVFKPYCSSA DLSSCSKESL INAYDNTIFY NDYLLDKIIS
     MLENAKQPAL MIYLSDHGES LGEEAFYLHG IPKSIAPKEQ YEIPFIVYAN EPFKEKHSII
     QTQTPINQNV IFHSVLGVFL DFKNPSVVYR PSLDLLKHKK E