ID   RFAP_ECOLX              Reviewed;         265 AA.
AC   Q9R9D6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Lipopolysaccharide core heptose(I) kinase RfaP;
DE            EC=2.7.1.-;
GN   Name=rfaP; Synonyms=waaP;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F470;
RX   PubMed=9792656; DOI=10.1074/jbc.273.45.29497;
RA   Heinrichs D.E., Yethon J.A., Amor P.A., Whitfield C.;
RT   "The assembly system for the outer core portion of R1- and R4-type
RT   lipopolysaccharides of Escherichia coli. The R1 core-specific beta-
RT   glucosyltransferase provides a novel attachment site for O-
RT   polysaccharides.";
RL   J. Biol. Chem. 273:29497-29505(1998).
RN   [2]
RP   FUNCTION IN LIPOPOLYSACCHARIDE CORE BIOSYNTHESIS.
RC   STRAIN=F470;
RX   PubMed=9756860; DOI=10.1074/jbc.273.41.26310;
RA   Yethon J.A., Heinrichs D.E., Monteiro M.A., Perry M.B., Whitfield C.;
RT   "Involvement of waaY, waaQ, and waaP in the modification of Escherichia
RT   coli lipopolysaccharide and their role in the formation of a stable outer
RT   membrane.";
RL   J. Biol. Chem. 273:26310-26316(1998).
RN   [3]
RP   FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   ASP-162.
RC   STRAIN=F470;
RX   PubMed=11069912; DOI=10.1074/jbc.m008255200;
RA   Yethon J.A., Whitfield C.;
RT   "Purification and characterization of WaaP from Escherichia coli, a
RT   lipopolysaccharide kinase essential for outer membrane stability.";
RL   J. Biol. Chem. 276:5498-5504(2001).
CC   -!- FUNCTION: Catalyzes the phosphorylation of heptose(I) of the outer
CC       membrane lipopolysaccharide core. {ECO:0000269|PubMed:11069912,
CC       ECO:0000269|PubMed:9756860}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11069912};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=76 uM for lipopolysaccharide acceptor
CC         {ECO:0000269|PubMed:11069912};
CC         KM=130 uM for ATP {ECO:0000269|PubMed:11069912};
CC         Vmax=3.7 nmol/min/mg enzyme {ECO:0000269|PubMed:11069912};
CC       pH dependence:
CC         Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:11069912};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC       family. {ECO:0000305}.
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DR   EMBL; AF019746; AAC69677.1; -; Genomic_DNA.
DR   RefSeq; WP_001295235.1; NZ_WVVZ01000013.1.
DR   AlphaFoldDB; Q9R9D6; -.
DR   SMR; Q9R9D6; -.
DR   STRING; 585034.ECIAI1_3800; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 1331937at2; -.
DR   UniPathway; UPA00958; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017172; Lsacc_core_hep_kinase_RfaP.
DR   PIRSF; PIRSF037318; RfaP; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipopolysaccharide biosynthesis; Magnesium;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..265
FT                   /note="Lipopolysaccharide core heptose(I) kinase RfaP"
FT                   /id="PRO_0000383676"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         162
FT                   /note="D->A: No activity."
FT                   /evidence="ECO:0000269|PubMed:11069912"
SQ   SEQUENCE   265 AA;  31051 MW;  1DB87969ACC679FD CRC64;
     MVELKEPFAT LWRGKDPFEE VKTLQGEVFR ELETRRTLRF EMAGKSYFLK WHRGTTLKEI
     IKNLLSLRMP VLGADREWNA IHRLRDVGVD TMYGVAFGEK GMNPLTRTSF IITEDLTPTI
     SLEDYCADWA TNPPDVRVKR MLIKRVATMV RDMHAAGINH RDCYICHFLL HLPFSGKEEE
     LKISVIDLHR AQLRTRVPRR WRDKDLIGLY FSSMNIGLTQ RDIWRFMKVY FAAPLKDILK
     QEQGLLSQAE AKATKIRERT IRKSL