EPTC_ECOLI
ID EPTC_ECOLI Reviewed; 577 AA.
AC P0CB39; P32678; Q2M8Q0; Q9S4U6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phosphoethanolamine transferase EptC;
DE EC=2.7.-.-;
GN Name=eptC; Synonyms=cptA, yijP; OrderedLocusNames=b3955, JW3927;
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=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
CC -!- FUNCTION: Catalyzes the addition of a phosphoethanolamine moiety to the
CC outer membrane lipopolysaccharide core. {ECO:0000250}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBUNIT: Forms a complex with an unidentified protein of approximately
CC 36 kDa. {ECO:0000269|PubMed:16079137}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137}.
CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family.
CC EptC/CptA subfamily. {ECO:0000305}.
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DR EMBL; U00006; AAC43061.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76937.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77356.1; -; Genomic_DNA.
DR PIR; F65202; F65202.
DR RefSeq; NP_418390.1; NC_000913.3.
DR RefSeq; WP_000556306.1; NZ_SSZK01000014.1.
DR PDB; 5ZZU; X-ray; 2.10 A; A/B/C=205-577.
DR PDB; 6A82; X-ray; 2.10 A; A/B/C=205-577.
DR PDB; 6A83; X-ray; 2.60 A; A=205-577.
DR PDBsum; 5ZZU; -.
DR PDBsum; 6A82; -.
DR PDBsum; 6A83; -.
DR AlphaFoldDB; P0CB39; -.
DR SMR; P0CB39; -.
DR BioGRID; 4260945; 16.
DR IntAct; P0CB39; 2.
DR STRING; 511145.b3955; -.
DR jPOST; P0CB39; -.
DR PaxDb; P0CB39; -.
DR PRIDE; P0CB39; -.
DR EnsemblBacteria; AAC76937; AAC76937; b3955.
DR EnsemblBacteria; BAE77356; BAE77356; BAE77356.
DR GeneID; 948458; -.
DR KEGG; ecj:JW3927; -.
DR KEGG; eco:b3955; -.
DR PATRIC; fig|1411691.4.peg.2750; -.
DR EchoBASE; EB1858; -.
DR eggNOG; COG2194; Bacteria.
DR HOGENOM; CLU_018534_3_3_6; -.
DR InParanoid; P0CB39; -.
DR OMA; PMYTIPF; -.
DR PhylomeDB; P0CB39; -.
DR BioCyc; EcoCyc:EG11914-MON; -.
DR BioCyc; MetaCyc:EG11914-MON; -.
DR UniPathway; UPA00958; -.
DR PRO; PR:P0CB39; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IMP:EcoCyc.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
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 3D-structure; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Lipopolysaccharide biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..577
FT /note="Phosphoethanolamine transferase EptC"
FT /id="PRO_0000209150"
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"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6A83"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 313..319
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:5ZZU"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 420..449
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:5ZZU"
FT TURN 508..512
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 520..528
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:5ZZU"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:5ZZU"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:5ZZU"
SQ SEQUENCE 577 AA; 66610 MW; 08465655D87CF75A 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 PFQEVLNDPA PKKLIIVHLL GTHIKYKYRY PENQGKFDGN TDHVPPGLNA
EELESYNDYD NANLYNDHVV ASLIKDFKAA NPNGFLVYFS DHGEEVYDTP PHKTQGRNED
NPTRHMYTIP FLLWTSEKWQ ATHPRDFSQD VDRKYSLAEL IHTWSDLAGL SYDGYDPTRS
VVNPQFKETT RWIGNPYKKN ALIDYDTLPY GDQVGNQ
