EPTB_ECOLI
ID EPTB_ECOLI Reviewed; 563 AA.
AC P37661; Q2M7K7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Kdo(2)-lipid A phosphoethanolamine 7''-transferase;
DE EC=2.7.8.42 {ECO:0000269|PubMed:15795227};
DE AltName: Full=Phosphoethanolamine transferase EptB;
GN Name=eptB; Synonyms=yhjW; OrderedLocusNames=b3546, JW5660;
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=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP C-TERMINUS.
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 PROTEIN SEQUENCE OF 220-231.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15795227; DOI=10.1074/jbc.m500964200;
RA Reynolds C.M., Kalb S.R., Cotter R.J., Raetz C.R.H.;
RT "A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-
RT octulosonic acid residue of Escherichia coli lipopolysaccharide.
RT Identification of the eptB gene and Ca2+ hypersensitivity of an eptB
RT deletion mutant.";
RL J. Biol. Chem. 280:21202-21211(2005).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Catalyzes the addition of a phosphoethanolamine (pEtN) moiety
CC to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a
CC Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl
CC group functions as pEtN donors and the reaction releases
CC diacylglycerol. {ECO:0000269|PubMed:15795227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + alpha-Kdo-
CC (2->4)-alpha-Kdo-(2->6)-lipid A = 7-O-[2-
CC aminoethoxy(hydroxy)phosphoryl]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-
CC lipid A + a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:24698,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:58540, ChEBI:CHEBI:60085,
CC ChEBI:CHEBI:64612; EC=2.7.8.42;
CC Evidence={ECO:0000269|PubMed:15795227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + alpha-Kdo-
CC (2->4)-alpha-Kdo-(2->6)-lipid IVA = 7-O-[2-
CC aminoethoxy(hydroxy)phosphoryl]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-
CC lipid IVA + a 1,2-diacyl-sn-glycerol; Xref=Rhea:RHEA:46908,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:60365, ChEBI:CHEBI:64612,
CC ChEBI:CHEBI:87107; EC=2.7.8.42;
CC Evidence={ECO:0000269|PubMed:15795227};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15795227};
CC -!- ACTIVITY REGULATION: Inhibited by calcium concentrations higher than 1
CC mM. {ECO:0000269|PubMed:15795227}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15795227}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15795227}.
CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptB
CC subfamily. {ECO:0000305}.
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DR EMBL; U00039; AAB18523.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76570.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77749.1; -; Genomic_DNA.
DR PIR; D65153; D65153.
DR RefSeq; NP_418002.2; NC_000913.3.
DR RefSeq; WP_001269197.1; NZ_SSZK01000068.1.
DR AlphaFoldDB; P37661; -.
DR SMR; P37661; -.
DR BioGRID; 4262537; 7.
DR BioGRID; 852376; 3.
DR IntAct; P37661; 5.
DR STRING; 511145.b3546; -.
DR jPOST; P37661; -.
DR PaxDb; P37661; -.
DR PRIDE; P37661; -.
DR EnsemblBacteria; AAC76570; AAC76570; b3546.
DR EnsemblBacteria; BAE77749; BAE77749; BAE77749.
DR GeneID; 948068; -.
DR KEGG; ecj:JW5660; -.
DR KEGG; eco:b3546; -.
DR PATRIC; fig|1411691.4.peg.3168; -.
DR EchoBASE; EB2176; -.
DR eggNOG; COG2194; Bacteria.
DR HOGENOM; CLU_018534_1_1_6; -.
DR InParanoid; P37661; -.
DR OMA; FAMQSEV; -.
DR PhylomeDB; P37661; -.
DR BioCyc; EcoCyc:EG12267-MON; -.
DR BioCyc; MetaCyc:EG12267-MON; -.
DR BRENDA; 2.7.8.42; 2026.
DR PRO; PR:P37661; -.
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:0043838; F:phosphatidylethanolamine:Kdo2-lipid A phosphoethanolamine transferase activity; IDA:EcoCyc.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..563
FT /note="Kdo(2)-lipid A phosphoethanolamine 7''-transferase"
FT /id="PRO_0000209148"
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..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..117
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..563
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 63804 MW; 40CF0E6A31779230 CRC64;
MRYIKSITQQ KLSFLLAIYI GLFMNGAVFY RRFGSYAHDF TVWKGISAVV ELAATVLVTF
FLLRLLSLFG RRSWRILASL VVLFSAGASY YMTFLNVVIG YGIIASVMTT DIDLSKEVVG
LNFILWLIAV SALPLILIWN NRCRYTLLRQ LRTPGQRIRS LAVVVLAGIM VWAPIRLLDI
QQKKVERATG VDLPSYGGVV ANSYLPSNWL SALGLYAWAR VDESSDNNSL LNPAKKFTYQ
APQNVDDTYV VFIIGETTRW DHMGIFGYER NTTPKLAQEK NLAAFRGYSC DTATKLSLRC
MFVRQGGAED NPQRTLKEQN IFAVLKQLGF SSDLYAMQSE MWFYSNTMAD NIAYREQIGA
EPRNRGKPVD DMLLVDEMQQ SLGRNPDGKH LIILHTKGSH FNYTQRYPRS FAQWKPECIG
VDSGCTKAQM INSYDNSVTY VDHFISSVID QVRDKKAIVF YAADHGESIN EREHLHGTPR
ELAPPEQFRV PMMVWMSDKY LENPANAQAF AQLKKEADMK VPRRHVELYD TIMGCLGYTS
PDGGINENNN WCHIPQAKEA AAN
