EPTB_SALTY
ID EPTB_SALTY Reviewed; 563 AA.
AC P43666;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Kdo(2)-lipid A phosphoethanolamine 7''-transferase;
DE EC=2.7.8.42 {ECO:0000250|UniProtKB:P37661};
DE AltName: Full=Phosphoethanolamine transferase EptB;
GN Name=eptB; OrderedLocusNames=STM3635;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=7721701; DOI=10.1128/jb.177.8.2087-2097.1995;
RA Baeumler A.J., Heffron F.;
RT "Identification and sequence analysis of lpfABCDE, a putative fimbrial
RT operon of Salmonella typhimurium.";
RL J. Bacteriol. 177:2087-2097(1995).
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:0000250|UniProtKB:P37661}.
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:0000250|UniProtKB:P37661};
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:0000250|UniProtKB:P37661};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptB
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73971.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL22495.1; -; Genomic_DNA.
DR EMBL; U18559; AAA73971.1; ALT_INIT; Genomic_DNA.
DR PIR; F56271; F56271.
DR RefSeq; NP_462536.1; NC_003197.2.
DR RefSeq; WP_001269259.1; NC_003197.2.
DR AlphaFoldDB; P43666; -.
DR SMR; P43666; -.
DR STRING; 99287.STM3635; -.
DR PaxDb; P43666; -.
DR EnsemblBacteria; AAL22495; AAL22495; STM3635.
DR GeneID; 1255159; -.
DR KEGG; stm:STM3635; -.
DR PATRIC; fig|99287.12.peg.3844; -.
DR HOGENOM; CLU_018534_1_1_6; -.
DR OMA; FAMQSEV; -.
DR PhylomeDB; P43666; -.
DR BioCyc; SENT99287:STM3635-MON; -.
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:0043838; F:phosphatidylethanolamine:Kdo2-lipid A phosphoethanolamine transferase activity; IBA:GO_Central.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..563
FT /note="Kdo(2)-lipid A phosphoethanolamine 7''-transferase"
FT /id="PRO_0000209149"
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; 64001 MW; 337AEA3E33FB5A43 CRC64;
MRYIKSMTQQ KLSFLLALYI GLFMNCAVFY RRFGSYAQEF TIWKGLSAVV ELGATVLVTF
FLLRLLSLFG RRVWRVLATL VVLFSAGASY YMTFLNVVIG YGIIASVMTT DIDLSKEVVG
LHFVLWLIAV SVLPLIFIWS NHCRYTLLRQ LRTPGQRFRS AAVVVLAGVM VWAPIRLLDI
QQKKVERATG IDLPSYGGVV ANSYLPSNWL SALGLYAWAQ VDESSDNNSL INPARKFTYV
APKDGDDTYV VFIIGETTRW DHMGIFGYER NTTPKLAQEK NLAAFRGYSC DTATKLSLRC
MFVREGGADN NPQRTLKEQN VFAVLKQLGF SSDLYAMQSE MWFYSNTMAD NISYREQIGA
EPRNRGKTVD DMLLIDEMQN SLAQNPEGKH LIILHTKGSH FNYTQRYPRS YAQWKPECIG
VDSGCTKAQM INSYDNSVTY VDHFITSVFD QLRDKKAIVF YAADHGESIN EREHLHGTPR
NMAPPEQFRV PMLVWMSDKY LASPQHAQMF AHLKQQAEIK VPRRHVELYD TIMGCLGYTS
PNGGINQNNN WCHIPDVQKV AAK
