ID   EPTA_SALTY              Reviewed;         547 AA.
AC   P36555;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Phosphoethanolamine transferase EptA;
DE            EC=2.7.-.-;
DE   AltName: Full=Polymyxin resistance protein PmrC;
GN   Name=eptA; Synonyms=pagB, pmrC; OrderedLocusNames=STM4293;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=8391535; DOI=10.1128/jb.175.13.4154-4164.1993;
RA   Roland K.L., Martin L.E., Esther C.R., Spitznagel J.K.;
RT   "Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-
RT   component regulatory system with a possible role in virulence.";
RL   J. Bacteriol. 175:4154-4164(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   INDUCTION.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=8955307; DOI=10.1128/jb.178.23.6857-6864.1996;
RA   Gunn J.S., Miller S.I.;
RT   "PhoP-PhoQ activates transcription of pmrAB, encoding a two-component
RT   regulatory system involved in Salmonella typhimurium antimicrobial peptide
RT   resistance.";
RL   J. Bacteriol. 178:6857-6864(1996).
RN   [4]
RP   INDUCTION.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=10480935; DOI=10.1074/jbc.274.38.27185;
RA   Woesten M.M.S.M., Groisman E.A.;
RT   "Molecular characterization of the PmrA regulon.";
RL   J. Biol. Chem. 274:27185-27190(1999).
RN   [5]
RP   FUNCTION.
RC   STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=11535603; DOI=10.1074/jbc.m106960200;
RA   Zhou Z., Ribeiro A.A., Lin S., Cotter R.J., Miller S.I., Raetz C.R.H.;
RT   "Lipid A modifications in polymyxin-resistant Salmonella typhimurium: pmrA-
RT   dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine
RT   incorporation.";
RL   J. Biol. Chem. 276:43111-43121(2001).
RN   [6]
RP   FUNCTION, INDUCTION BY BASR, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=15205413; DOI=10.1128/jb.186.13.4124-4133.2004;
RA   Lee H., Hsu F.-F., Turk J., Groisman E.A.;
RT   "The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of
RT   lipid A and polymyxin resistance in Salmonella enterica.";
RL   J. Bacteriol. 186:4124-4133(2004).
CC   -!- FUNCTION: Catalyzes the addition of a phosphoethanolamine moiety to the
CC       lipid A. The phosphoethanolamine modification is required for
CC       resistance to polymyxin. {ECO:0000269|PubMed:11535603,
CC       ECO:0000269|PubMed:15205413}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:15205413}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15205413}.
CC   -!- INDUCTION: The eptA-basRS operon is positively autoregulated by BasR
CC       under high iron or aluminum concentration conditions.
CC       {ECO:0000269|PubMed:10480935, ECO:0000269|PubMed:15205413,
CC       ECO:0000269|PubMed:8955307}.
CC   -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L13395; AAA72364.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL23117.1; -; Genomic_DNA.
DR   PIR; A40656; A40656.
DR   RefSeq; NP_463158.1; NC_003197.2.
DR   RefSeq; WP_000919289.1; NC_003197.2.
DR   AlphaFoldDB; P36555; -.
DR   SMR; P36555; -.
DR   STRING; 99287.STM4293; -.
DR   PaxDb; P36555; -.
DR   EnsemblBacteria; AAL23117; AAL23117; STM4293.
DR   GeneID; 1255819; -.
DR   KEGG; stm:STM4293; -.
DR   PATRIC; fig|99287.12.peg.4515; -.
DR   HOGENOM; CLU_018534_1_0_6; -.
DR   OMA; NSIAFYF; -.
DR   PhylomeDB; P36555; -.
DR   BioCyc; SENT99287:STM4293-MON; -.
DR   BRENDA; 2.7.8.43; 2169.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001014; 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: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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane;
KW   Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..547
FT                   /note="Phosphoethanolamine transferase EptA"
FT                   /id="PRO_0000209152"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..47
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..79
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..123
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..547
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   547 AA;  61619 MW;  A9E2E2B146B7A78C CRC64;
     MLKRFLKRPV LGQIAWLLLF SFYIAVCLNI AFYKQVLQDL PLNSLRNVLV FISMPVVAFS
     VVNSVLTLAS FIWLNRLLAC VFILVGAAAQ YFILTYGIII DRSMIANMMD TTPAETFALM
     TPQMVLTLGL SGVLAAVIAF WVKIRPATPR LRSGLYRLAS VLISILLVIL VAAFFYKDYA
     SLFRNNKQLI KALSPSNSIV ASWSWYSHQR LANLPLVRIG EDAHRNPLML KGDRKNLTIL
     IVGETSRGDD FSLGGYPRDT NPRLAKDDVI YFPHTTSCGT ATAISVPCMF SDMPRKHYDE
     ELAHHQEGLL DIIQRAGINV LWNDNDGGCK GACDRVPHQN VTELNLPGQC IDGECYDEVL
     FHGLEDYIDH LKGDGVIVLH TIGSHGPTYY NRYPPQFKKF TPTCDTNEIQ NCSQEQLINT
     YDNTVLYVDY IVDKAINLLK SHQDKFTTSL VYLSDHGESL GENGVYLHGL PYSIAPDTQK
     HVPMLIWLSK DYQQRYQVDQ ACLQKRASTL DYSQDNLFST MLGLTGVQTT YYQAADDILQ
     PCRRLSE