ID A0A1A0FM09_9GAMM Unreviewed; 237 AA.
AC A0A1A0FM09;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ADS46_10040 {ECO:0000313|EMBL:OBA00517.1};
OS Halomonas sp. G11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1684425 {ECO:0000313|EMBL:OBA00517.1, ECO:0000313|Proteomes:UP000092250};
RN [1] {ECO:0000313|EMBL:OBA00517.1, ECO:0000313|Proteomes:UP000092250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G11 {ECO:0000313|EMBL:OBA00517.1,
RC ECO:0000313|Proteomes:UP000092250};
RA Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA Eddine Masmoudi A.S., Cherif A.;
RT "Genomic basis for crude oil degradation, heavy metal resistance and high
RT salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT Tunisian Chott El-Djerid salt lake.";
RL Submitted (FEB-2016) 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:OBA00517.1}.
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DR EMBL; LYXG01000003; OBA00517.1; -; Genomic_DNA.
DR RefSeq; WP_066315551.1; NZ_LYXG01000003.1.
DR AlphaFoldDB; A0A1A0FM09; -.
DR OrthoDB; 6854449at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000092250; 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:OBA00517.1};
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 Transferase {ECO:0000256|HAMAP-Rule:MF_00521}.
FT ACT_SITE 175
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ SEQUENCE 237 AA; 26588 MW; 24575F6A4C8FB580 CRC64;
MRLAALRQGN SLILHDADSL CDAAMSHQPD PALFSAEYWR SRDLVVGEAP GRGSSLFLQA
NPSEQWVLRP YRRGGLVAKL SQKRYFWVGA ERTRGFREMR LTANLFEQGL PVPRPIATCV
ARHGLSYEAA LITQRITGGK ALAELIVSHL ADEALLQRVG AMIRRFHRAK LDHVDLNARN
ILVDASGAPW LIDLDRCRLR QPGKWQNANL ERLERSIHKF DSTLSTSPIL QGYRATG
//