ID K0C808_CYCSP Unreviewed; 267 AA.
AC K0C808;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Lipopolysaccharide core heptose(I) kinase {ECO:0000256|PIRNR:PIRNR037318};
DE EC=2.7.1.- {ECO:0000256|PIRNR:PIRNR037318};
GN Name=waaP {ECO:0000313|EMBL:AFT67802.1};
GN OrderedLocusNames=Q91_1768 {ECO:0000313|EMBL:AFT67802.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT67802.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT67802.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT67802.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(2012).
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; CP003230; AFT67802.1; -; Genomic_DNA.
DR RefSeq; WP_015006571.1; NC_018697.1.
DR AlphaFoldDB; K0C808; -.
DR STRING; 385025.Q91_1768; -.
DR KEGG; cyq:Q91_1768; -.
DR PATRIC; fig|385025.3.peg.1806; -.
DR HOGENOM; CLU_081267_0_0_6; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000006282; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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, ECO:0000313|EMBL:AFT67802.1};
KW Lipopolysaccharide biosynthesis {ECO:0000256|PIRNR:PIRNR037318};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037318};
KW Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW Transferase {ECO:0000256|PIRNR:PIRNR037318}.
SQ SEQUENCE 267 AA; 31182 MW; 04C454BE0C162511 CRC64;
MKLEVTEEFQ KDWGDTPSFD QLMALDGEMY RQVARRKTFK FLLKETFYFA KIHHGVGWRE
ILKNIIQGRL PILGAENEYD AIRALTKLGI KTMTLAAYGR RGWNIAEQES FVLTRSLEPA
ISLEDFCANW AVDKPSLKLK RALIRRVASI TRKMHENGIN HRDLYICHFL LKENELEALN
GNKDVDLYLI DLHRVQIRAK TPMRWLVKDL AALWFSSMDL GLSRQDLFYF IHHYTGNKAT
KELTGNKKFW AEVKRKARIL KAKPIKA
//
