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Database: UniProt
Entry: Q1R4W3_ECOUT
LinkDB: Q1R4W3_ECOUT
Original site: Q1R4W3_ECOUT 
ID   Q1R4W3_ECOUT            Unreviewed;       268 AA.
AC   Q1R4W3;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Lipopolysaccharide core heptose(I) kinase {ECO:0000256|PIRNR:PIRNR037318};
DE            EC=2.7.1.- {ECO:0000256|PIRNR:PIRNR037318};
GN   Name=rfaP {ECO:0000313|EMBL:ABE09601.1};
GN   OrderedLocusNames=UTI89_C4173 {ECO:0000313|EMBL:ABE09601.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09601.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE09601.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Kinase involved in the biosynthesis of the core
CC       oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the
CC       phosphorylation of heptose I (HepI), the first heptose added to the
CC       Kdo2-lipid A module. {ECO:0000256|PIRNR:PIRNR037318}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR037318}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/rfaP
CC       family. {ECO:0000256|PIRNR:PIRNR037318}.
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DR   EMBL; CP000243; ABE09601.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1R4W3; -.
DR   KEGG; eci:UTI89_C4173; -.
DR   HOGENOM; CLU_081267_0_0_6; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
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   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 {ECO:0000256|PIRNR:PIRNR037318};
KW   Kinase {ECO:0000256|PIRNR:PIRNR037318};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|PIRNR:PIRNR037318};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037318};
KW   Transferase {ECO:0000256|PIRNR:PIRNR037318, ECO:0000313|EMBL:ABE09601.1}.
SQ   SEQUENCE   268 AA;  31448 MW;  C15B193CDA5737DA CRC64;
     MVWMVELKEP FATLWRGKDP FEEVKTLQGE VFRELETRRT LRFEMAGKSY FLKWHRGTTL
     KEIIKNLLSL RMPVLGADRE WNAIHRLRDV GVDTMYGVAF GEKGINPLTR TSFIITEDLT
     PTISLEDYCA DWATNPPDVR VKRMLIKRVA TMVRDMHAAG INHRDCYICH FLLHLPFSGK
     EEVLKISVID LHRAQIRAKV PRRWRDKDLI GLYFSSMNIG LTQRDIWRFM KVYFVAPLKD
     IIKQEQGLLS QAEEKATKIR ERTIRKSL
//
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