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Database: UniProt
Entry: A3QJC4_SHELP
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ID   A3QJC4_SHELP            Unreviewed;       241 AA.
AC   A3QJC4;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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   OrderedLocusNames=Shew_3706 {ECO:0000313|EMBL:ABO25572.1};
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO25572.1, ECO:0000313|Proteomes:UP000001558};
RN   [1] {ECO:0000313|EMBL:ABO25572.1, ECO:0000313|Proteomes:UP000001558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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}.
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DR   EMBL; CP000606; ABO25572.1; -; Genomic_DNA.
DR   RefSeq; WP_011867500.1; NC_009092.1.
DR   AlphaFoldDB; A3QJC4; -.
DR   STRING; 323850.Shew_3706; -.
DR   KEGG; slo:Shew_3706; -.
DR   eggNOG; COG0478; Bacteria.
DR   HOGENOM; CLU_094226_0_0_6; -.
DR   OrthoDB; 6854449at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001558; Chromosome.
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:ABO25572.1};
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:UP000001558};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00521}.
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   241 AA;  27502 MW;  C0F940741DD41D04 CRC64;
     MQIKPTDAGC IVFSQASLKA ITPDWFTFDY WQDLGAITGS SKGRYTTWFV NPAPLSQAPE
     EEWVLRHYYR GGMMEKFSRD AYLYTGLKRC RAIAEFNLLE QLFKEGFAVP EPVAAQIQRS
     GPYYRGDIII KRIPGARDLV AELSQGPMSD EKWQALGACI AKFHRRGVYH ADLNAKNILL
     AGENFTLIDF DRGELKQPDS KWQQSNLDRL LRSFNKEKGK APELHFSQEN WQLLLAGYAQ
     A
//
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