ID A0A2A5GB18_9GAMM Unreviewed; 271 AA.
AC A0A2A5GB18;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Lipopolysaccharide core heptose(I) kinase {ECO:0000256|PIRNR:PIRNR037318};
DE EC=2.7.1.- {ECO:0000256|PIRNR:PIRNR037318};
GN ORFNames=COA46_11905 {ECO:0000313|EMBL:PCJ90223.1};
OS Porticoccaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae.
OX NCBI_TaxID=2026782 {ECO:0000313|EMBL:PCJ90223.1, ECO:0000313|Proteomes:UP000230152};
RN [1] {ECO:0000313|Proteomes:UP000230152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCJ90223.1}.
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DR EMBL; NVXH01000013; PCJ90223.1; -; Genomic_DNA.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000230152; Unassembled WGS sequence.
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, ECO:0000313|EMBL:PCJ90223.1};
KW Lipopolysaccharide biosynthesis {ECO:0000256|PIRNR:PIRNR037318};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037318};
KW Transferase {ECO:0000256|PIRNR:PIRNR037318}.
SQ SEQUENCE 271 AA; 31303 MW; 0D5665BC86C0BDB4 CRC64;
MKLFLAEPFA SKWENNDPFD VAFSLTGETY RDMGDRCTTR FEFGNKAYFV KTHSGVGVGE
ILKNLLYLRM PVLGAENEYQ AIGRLNELGV ETMTAKAFGR TGWNPASEKS FLITDALEPT
EPLDEYCNPA VLFEMGVSAR RALVRRLAKI SRTLHDSGVN HRDYYLCHFL LDTSEDFIDV
PVFKRPIYLI DLHRVQLRNR TPRRWRQKDL SALYYSARRV GFDQRDVLCF IRXYKQQPLS
KALSDKINFW HAIGRAADKL HDKGVRKGYH G
//