ID   EPTC_ECOLX              Reviewed;         577 AA.
AC   P0CB40; P32678; Q2M8Q0; Q9S4U6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Phosphoethanolamine transferase EptC;
DE            EC=2.7.-.-;
GN   Name=eptC; Synonyms=cptA, yijP;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN PATHOGENESIS.
RC   STRAIN=K1 / RS218 / O18:K1:H7;
RX   PubMed=10456927; DOI=10.1128/iai.67.9.4751-4756.1999;
RA   Wang Y., Huang S.-H., Wass C.A., Stins M.F., Kim K.S.;
RT   "The gene locus yijP contributes to Escherichia coli K1 invasion of brain
RT   microvascular endothelial cells.";
RL   Infect. Immun. 67:4751-4756(1999).
CC   -!- FUNCTION: Catalyzes the addition of a phosphoethanolamine moiety to the
CC       outer membrane lipopolysaccharide core (By similarity). Plays a role in
CC       the pathogenesis of E.coli meningitis. Required for invasion of E.coli
CC       K1 into brain microvascular endothelial cells (BMEC). Contributes to
CC       E.coli traversal across the blood-brain barrier. {ECO:0000250,
CC       ECO:0000269|PubMed:10456927}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family.
CC       EptC/CptA subfamily. {ECO:0000305}.
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DR   EMBL; AF112861; AAD28716.1; -; Genomic_DNA.
DR   RefSeq; WP_000556298.1; NZ_WWEV01000117.1.
DR   AlphaFoldDB; P0CB40; -.
DR   SMR; P0CB40; -.
DR   STRING; 585034.ECIAI1_4163; -.
DR   eggNOG; COG2194; Bacteria.
DR   OMA; PMYTIPF; -.
DR   OrthoDB; 1067869at2; -.
DR   UniPathway; UPA00958; -.
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   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR040423; PEA_transferase.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR30443; PTHR30443; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Lipopolysaccharide biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..577
FT                   /note="Phosphoethanolamine transferase EptC"
FT                   /id="PRO_0000383951"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   577 AA;  66670 MW;  D1D6D70EEE2DE5C1 CRC64;
     MHSTEVQAKP LFSWKALGWA LLYFWFFSTL LQAIIYISGY SGTNGIRDSL LFSSLWLIPV
     FLFPKRIKII AAVIGVVLWA ASLAALCYYV IYGQEFSQSV LFVMFETNTN EASEYLSQYF
     SLKIVLIALA YTAVAVLLWT RLRPVYIPKP WRYVVSFALL YGLILHPIAM NTFIKNKPFE
     KTLDNLASRM EPAAPWQFLT GYYQYRQQLN SLTKLLNENN ALPPLANFKD ESGNEPRTLV
     LVIGESTQRG RMSLYGYPRE TTPELDALHK TDPNLTVFNN VVTSRPYTIE ILQQALTFAN
     EKNPDLYLTQ PSLMNMMKQA GYKTFWITNQ QTMTARNTML TVFSRQTDKQ YYMNQQRTQS
     AREYDTNVLK PFQEVLKDPA PKKLIIVHLL GTHIKYKYRY PEDQGKFDGN TEHVPPGLNA
     EELESYNDYD NANLYNDHVV ASLIKDFKAT DPNGFLVYFS DHGEEVYDTP PHKTQGRNED
     NPTRHMYTIP FLLWTSEKWQ ATHPRDFSQD VDRKYSLAEL IHTWSDLAGL SYDGYDPTRS
     VVNPQFKETT RWIGNPYKKN ALIDYDTLPY GDQVGNQ