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
//