ID   WAAP_ECOLI              Reviewed;         265 AA.
AC   P25741; Q2M7U4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-SEP-2026, entry version 154.
DE   RecName: Full=Lipopolysaccharide core heptose(I) kinase WaaP {ECO:0000250|UniProtKB:Q9R9D6};
DE            EC=2.7.1.235 {ECO:0000250|UniProtKB:Q9R9D6};
GN   Name=waaP {ECO:0000303|PubMed:9004408};
GN   Synonyms=rfaP {ECO:0000303|PubMed:1732225};
GN   OrderedLocusNames=b3630, JW3605;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1732225; DOI=10.1128/jb.174.3.930-934.1992;
RA   Parker C.T., Pradel E., Schnaitman C.A.;
RT   "Identification and sequences of the lipopolysaccharide core biosynthetic
RT   genes rfaQ, rfaP, and rfaG of Escherichia coli K-12.";
RL   J. Bacteriol. 174:930-934(1992).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NOMENCLATURE.
RX   PubMed=9004408; DOI=10.1016/s0966-842x(97)82912-5;
RA   Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D.,
RA   Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D.;
RT   "Bacterial polysaccharide synthesis and gene nomenclature.";
RL   Trends Microbiol. 4:495-503(1996).
CC   -!- FUNCTION: Kinase involved in the biosynthesis of the core
CC       oligosaccharide region of lipopolysaccharide (LPS) (By similarity).
CC       Catalyzes the phosphorylation of heptose I (HepI), the first heptose
CC       added to the Kdo2-lipid A module (By similarity).
CC       {ECO:0000250|UniProtKB:Q9R9D6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-D-Hep-(1->3)-L-alpha-D-Hep-(1->5)-[alpha-Kdo-
CC         (2->4)]-alpha-Kdo-(2->6)-lipid A + ATP = an L-alpha-D-Hep-(1->3)-4-O-
CC         phospho-L-alpha-D-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-
CC         lipid A + ADP + H(+); Xref=Rhea:RHEA:74087, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:193069, ChEBI:CHEBI:193070,
CC         ChEBI:CHEBI:456216; EC=2.7.1.235;
CC         Evidence={ECO:0000250|UniProtKB:Q9R9D6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alpha-D-Hep-(1->3)-L-alpha-D-Hep-(1->5)-[alpha-Kdo-(2->4)]-
CC         alpha-Kdo-(2->6)-lipid A (E. coli) + ATP = L-alpha-D-Hep-(1->3)-4-O-
CC         phospho-L-alpha-D-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-
CC         lipid A (E. coli) + ADP + H(+); Xref=Rhea:RHEA:74091,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61507,
CC         ChEBI:CHEBI:193075, ChEBI:CHEBI:456216; EC=2.7.1.235;
CC         Evidence={ECO:0000250|UniProtKB:Q9R9D6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9R9D6};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9R9D6}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC       family. {ECO:0000305}.
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DR   EMBL; M80599; AAA24083.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18607.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76654.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77662.1; -; Genomic_DNA.
DR   PIR; C42595; C42595.
DR   RefSeq; NP_418087.1; NC_000913.3.
DR   RefSeq; WP_000229840.1; NZ_CP009789.1.
DR   AlphaFoldDB; P25741; -.
DR   SMR; P25741; -.
DR   BioGRID; 4260804; 387.
DR   FunCoup; P25741; 61.
DR   IntAct; P25741; 7.
DR   STRING; 511145.b3630; -.
DR   jPOST; P25741; -.
DR   PaxDb; 511145-b3630; -.
DR   EnsemblBacteria; AAC76654; AAC76654; b3630.
DR   GeneID; 948150; -.
DR   KEGG; ecj:JW3605; -.
DR   KEGG; eco:b3630; -.
DR   KEGG; ecoc:C3026_19675; -.
DR   PATRIC; fig|1411691.4.peg.3076; -.
DR   EchoBASE; EB1316; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_081267_0_0_6; -.
DR   InParanoid; P25741; -.
DR   OMA; GWGEIFK; -.
DR   OrthoDB; 9782725at2; -.
DR   PhylomeDB; P25741; -.
DR   BioCyc; EcoCyc:EG11340-MONOMER; -.
DR   BioCyc; MetaCyc:EG11340-MONOMER; -.
DR   BRENDA; 2.7.1.B23; 2026.
DR   UniPathway; UPA00958; -.
DR   PRO; PR:P25741; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P25741; -.
DR   GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IDA:EcoCyc.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IDA:EcoCyc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017172; Lsacc_core_hep_kinase_RfaP.
DR   NCBIfam; NF011703; PRK15123.1; 1.
DR   Pfam; PF06293; Kdo; 1.
DR   PIRSF; PIRSF037318; RfaP; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Lipopolysaccharide biosynthesis; Magnesium;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..265
FT                   /note="Lipopolysaccharide core heptose(I) kinase WaaP"
FT                   /id="PRO_0000097285"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRS2"
SQ   SEQUENCE   265 AA;  30872 MW;  E77F1E9956ABDBED CRC64;
     MVELKEPLAT LWRGKDAFAE VKKLNGEVFR ELETRRTLRF ELSGKSYFLK WHKGTTLKEI
     IKNLLSLRMP VLGADREWHA IHRLSDVGVD TMKGIGFGEK GLNPLTRASF IITEDLTPTI
     SLEDYCADWA VNPPDIRVKR MLIARVATMV RKMHTAGINH RDCYICHFLL HLPFTGREDE
     LKISVIDLHR AQIRAKVPRR WRDKDLIGLY FSSMNIGLTQ RDIWRFMKVY FGMPLRKILS
     LEQNLLNMAS VKAERIKERT QRKGL
//