KDKA_HAEIN
ID KDKA_HAEIN Reviewed; 241 AA.
AC O86224; Q9F438;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid kinase;
DE Short=Kdo kinase;
DE EC=2.7.1.166;
GN Name=kdkA; OrderedLocusNames=HI_0260.1;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, KINETIC PARAMETERS, GENE NAME, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10531340; DOI=10.1074/jbc.274.44.31391;
RA White K.A., Lin S., Cotter R.J., Raetz C.R.H.;
RT "A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-
RT manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo
RT phosphorylation in bacterial virulence.";
RL J. Biol. Chem. 274:31391-31400(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd, and I69 / Serotype B;
RX PubMed=10952982; DOI=10.1074/jbc.m005204200;
RA Brabetz W., Mueller-Loennies S., Brade H.;
RT "3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and Kdo
RT kinase (KdkA) of Haemophilus influenzae are both required to complement a
RT waaA knockout mutation of Escherichia coli.";
RL J. Biol. Chem. 275:34954-34962(2000).
RN [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, PH DEPENDENCE, AND SUBCELLULAR LOCATION.
RC STRAIN=722;
RX PubMed=9195966; DOI=10.1074/jbc.272.26.16555;
RA White K.A., Kaltashov I.A., Cotter R.J., Raetz C.R.;
RT "A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a
RT Kdo kinase in extracts of Haemophilus influenzae.";
RL J. Biol. Chem. 272:16555-16563(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [5]
RP IDENTIFICATION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D., Peterson J.,
RA Hickey E., Dodson R., Gwinn M.;
RL Submitted (MAY-1998) 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. To a lesser extent, can use GTP instead of ATP as substrate.
CC {ECO:0000269|PubMed:10531340, ECO:0000269|PubMed:10952982,
CC ECO:0000269|PubMed:9195966}.
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:0000269|PubMed:10531340};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.6 uM for Kdo-lipid IV(A) {ECO:0000269|PubMed:10531340};
CC Vmax=73625 nmol/min/mg enzyme {ECO:0000269|PubMed:10531340};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9195966};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:10531340,
CC ECO:0000305|PubMed:9195966}; Peripheral membrane protein
CC {ECO:0000305|PubMed:10531340, ECO:0000305|PubMed:9195966}; Cytoplasmic
CC side {ECO:0000305|PubMed:10531340, ECO:0000305|PubMed:9195966}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY043284; AAK92207.1; -; Genomic_DNA.
DR EMBL; AJ277816; CAC07180.1; -; Genomic_DNA.
DR EMBL; AJ277817; CAC07181.1; -; Genomic_DNA.
DR EMBL; L42023; AAC21931.1; -; Genomic_DNA.
DR RefSeq; NP_438429.1; NC_000907.1.
DR RefSeq; WP_005694044.1; NC_000907.1.
DR AlphaFoldDB; O86224; -.
DR SMR; O86224; -.
DR STRING; 71421.HI_0260.1; -.
DR EnsemblBacteria; AAC21931; AAC21931; HI_0260.1.
DR KEGG; hin:HI_0260.1; -.
DR PATRIC; fig|71421.8.peg.275; -.
DR eggNOG; COG3642; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR OMA; YYRGGLW; -.
DR BioCyc; HINF71421:G1GJ1-275-MON; -.
DR BioCyc; MetaCyc:MON-15507; -.
DR BRENDA; 2.7.1.166; 2529.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000579; 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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Lipopolysaccharide biosynthesis; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..241
FT /note="3-deoxy-D-manno-octulosonic acid kinase"
FT /id="PRO_0000194313"
FT ACT_SITE 171
FT /evidence="ECO:0000255"
FT VARIANT 46
FT /note="I -> T (in strain: I69)"
FT VARIANT 85
FT /note="E -> D (in strain: I69)"
FT VARIANT 151..153
FT /note="TWM -> IWR (in strain: I69)"
FT VARIANT 200..201
FT /note="SA -> LG (in strain: I69)"
SQ SEQUENCE 241 AA; 28569 MW; 897A905BBA4BED09 CRC64;
MHQFQQDNQY FIFNFDRTFE QATEFFQAEF WQKQERVIGS AKGRGITYFL QTEDWFGVNC
ALRHYYRGGL WGKLNKDRYR FSALETTRSF AEFHLLQRLY EAGLPVPKPI AARIQKGKLG
ICYQADILTE KIENAQDLTA LLQTQTLPKE TWMQIGRLIR KLHDLQICHT DLNAHNILLQ
QTEQGQKCWL LDFDKCGEKS ADFWKVQNLN RLKRSFEKEV GRMNIQFTEQ NWADLTSAYH
Q
