KDKA_ACTSZ
ID KDKA_ACTSZ Reviewed; 240 AA.
AC A6VQT5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid kinase {ECO:0000255|HAMAP-Rule:MF_00521};
DE Short=Kdo kinase {ECO:0000255|HAMAP-Rule:MF_00521};
DE EC=2.7.1.166 {ECO:0000255|HAMAP-Rule:MF_00521};
GN Name=kdkA {ECO:0000255|HAMAP-Rule:MF_00521}; OrderedLocusNames=Asuc_1985;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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:0000255|HAMAP-Rule:MF_00521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->6)-lipid IVA + ATP = 4-O-phospho-alpha-Kdo-
CC (2->6)-lipid IVA + ADP + H(+); Xref=Rhea:RHEA:28506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:61589, ChEBI:CHEBI:456216; EC=2.7.1.166;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00521};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00521}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00521}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00521}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00521}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC family. {ECO:0000255|HAMAP-Rule:MF_00521}.
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DR EMBL; CP000746; ABR75332.1; -; Genomic_DNA.
DR RefSeq; WP_012073709.1; NC_009655.1.
DR AlphaFoldDB; A6VQT5; -.
DR STRING; 339671.Asuc_1985; -.
DR PRIDE; A6VQT5; -.
DR EnsemblBacteria; ABR75332; ABR75332; Asuc_1985.
DR KEGG; asu:Asuc_1985; -.
DR eggNOG; COG3642; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR OMA; YYRGGLW; -.
DR OrthoDB; 1643499at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001114; 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 HAMAP; MF_00521; KDO_kinase; 1.
DR InterPro; IPR022826; KDO_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Lipopolysaccharide biosynthesis; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..240
FT /note="3-deoxy-D-manno-octulosonic acid kinase"
FT /id="PRO_1000072491"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ SEQUENCE 240 AA; 28285 MW; C6C9D969FC61AF15 CRC64;
MLEIRQNHCF YLFNWDEPRQ DQTRFFSPEF WRRQGRISGT AQGRGITWFL QTVDLFGVNA
ALRHYYRGGL WGKINRDRYT FTSLENTRSF AEFRLLSRLH QAGMPVPKPL AAKVEKLSLG
GYRADILTEK VENARDLTAL LQTENLSDEA WRQIGKLIRR LHDLQICHTD LNAHNILVQQ
VKEQEKYWLL DFDKCGEKSG DFWKAQNLAR LKRSFLKEAA RMGIRFTEGD WKNLLKGYQN
