EPTA_ECO57
ID EPTA_ECO57 Reviewed; 547 AA.
AC A0A0H3JML2;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Phosphoethanolamine transferase EptA;
DE EC=2.7.-.- {ECO:0000305|PubMed:16514146};
DE AltName: Full=Polymyxin resistance protein PmrC;
GN Name=eptA; Synonyms=pmrC; OrderedLocusNames=ECs_5096;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=O157:H7 / 4304, and O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=16514146; DOI=10.1099/mic.0.28692-0;
RA Kim S.H., Jia W., Parreira V.R., Bishop R.E., Gyles C.L.;
RT "Phosphoethanolamine substitution in the lipid A of Escherichia coli
RT O157:H7 and its association with PmrC.";
RL Microbiology 152:657-666(2006).
CC -!- FUNCTION: There are several lipid A forms in this strain, including a
CC phosphoethanolamine (1-O-P-pEtN) form; overexpression of this gene
CC leads to higher levels of the 1-O-P-pEtN form of lipid A.
CC {ECO:0000269|PubMed:16514146}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P30845}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Decreased amounts of the 1-O-P-PEtN form of lipid
CC A. {ECO:0000269|PubMed:16514146}.
CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptA
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000007; BAB38519.2; -; Genomic_DNA.
DR RefSeq; NP_313123.2; NC_002695.1.
DR RefSeq; WP_001302789.1; NZ_SDVX01000004.1.
DR AlphaFoldDB; A0A0H3JML2; -.
DR SMR; A0A0H3JML2; -.
DR STRING; 155864.EDL933_5459; -.
DR EnsemblBacteria; BAB38519; BAB38519; ECs_5096.
DR GeneID; 914018; -.
DR KEGG; ecs:ECs_5096; -.
DR PATRIC; fig|386585.9.peg.5326; -.
DR eggNOG; COG2194; Bacteria.
DR HOGENOM; CLU_018534_1_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
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; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..547
FT /note="Phosphoethanolamine transferase EptA"
FT /id="PRO_0000446241"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 547 AA; 61766 MW; 5A80405B0BF4FD0D CRC64;
MLKRLLKRPS LNLLAWLLLA AFYISICLNI AFFKQVLQAL PLDSLHNVLV FLSMPVVAFS
VINIVLTLSS FLWLNRPLAC LFILVGAAAQ YFIMTYGIVI DRSMIANIID TTPAESYALM
TPQMLLTLGF SGVLAALIAC WIKIKPATSR LRSVLFRGAN ILVSVLLILL VAALFYKDYA
SLFRNNKELV KSLSPSNSIV ASWSWYSHQR LANLPLVRIG EDAHRNPLMQ NEKRKNLTIL
IVGETSRAEN FSLNGYPRET NPRLAKDNVV YFPNTASCGT ATAVSVPCMF SDMPREHYKE
ELAQHQEGVL DIIQRAGINV LWNDNDGGCK GACDRVPHQN VTALNLPDQC INGECYDEVL
FHGLEEYINN LQGDGVIVLH TIGSHRPTYY NRYPPQFRKF TPTCDTNEIQ TCTKEQLVNT
YDNTLVYVDY IVDKAINLLK EHQDKFTTSL VYLSDHGESL GENGIYLHGL PYAIAPDSQK
QVPMLLWLSE DYQKRYQVDQ NCLQKQAQTQ HYSQDNLFST LLGLTGVETK YYQAADDILQ
TCRRVSE