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Database: UniProt
Entry: A0A231HKA0_9BURK
LinkDB: A0A231HKA0_9BURK
Original site: A0A231HKA0_9BURK 
ID   A0A231HKA0_9BURK        Unreviewed;       236 AA.
AC   A0A231HKA0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid kinase {ECO:0000256|ARBA:ARBA00029511, ECO:0000256|HAMAP-Rule:MF_00521};
DE            Short=Kdo kinase {ECO:0000256|HAMAP-Rule:MF_00521};
DE            EC=2.7.1.166 {ECO:0000256|ARBA:ARBA00011988, ECO:0000256|HAMAP-Rule:MF_00521};
GN   Name=kdkA {ECO:0000256|HAMAP-Rule:MF_00521};
GN   ORFNames=PuT2_09560 {ECO:0000313|EMBL:OXR49300.1};
OS   Pusillimonas sp. T2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=1548123 {ECO:0000313|EMBL:OXR49300.1, ECO:0000313|Proteomes:UP000216496};
RN   [1] {ECO:0000313|EMBL:OXR49300.1, ECO:0000313|Proteomes:UP000216496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2 {ECO:0000313|EMBL:OXR49300.1,
RC   ECO:0000313|Proteomes:UP000216496};
RA   Yuan M., Qiu J.G., Ma Y.;
RT   "The genome sequence of Pusillimonas sp. T2.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-
CC       manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH
CC       position. {ECO:0000256|HAMAP-Rule:MF_00521}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-
CC         (2->6)-lipid IVA + ADP + H(+); Xref=Rhea:RHEA:74271,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:176428,
CC         ChEBI:CHEBI:193140, ChEBI:CHEBI:456216; EC=2.7.1.166;
CC         Evidence={ECO:0000256|ARBA:ARBA00034417, ECO:0000256|HAMAP-
CC         Rule:MF_00521};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713, ECO:0000256|HAMAP-Rule:MF_00521}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00521}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00521}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00521}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC       family. {ECO:0000256|ARBA:ARBA00010327, ECO:0000256|HAMAP-
CC       Rule:MF_00521}.
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:OXR49300.1}.
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DR   EMBL; NIQA01000004; OXR49300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231HKA0; -.
DR   OrthoDB; 6854449at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000216496; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   HAMAP; MF_00521; KDO_kinase; 1.
DR   InterPro; IPR022826; KDO_kinase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF06293; Kdo; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00521, ECO:0000313|EMBL:OXR49300.1};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216496};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00521}.
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   236 AA;  25909 MW;  C8C39FED3F7B3378 CRC64;
     MFKPEGFGVS ASAGPVVNVS GLSLDQTASW VGLFDPANPA LHAQPVQSGG RQSAWFIDGP
     MGAALLRHYR RGGLVAKFSK NRYLWQGARR TRAFAEFCLL DTMFRQGLPV PQPLAAAYWR
     HGLTYRAAIV VARIPHVMPL ADCLAQADPV AVAAAVLKIH DADVWHADLN AFNILLNAAG
     HVWVIDFDRG ESRGMSRALR NANLQRLRRS LVKVAAQQGE RFWQAVNVAY WQLATA
//
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