ID   KDSB2_ACTP2             Reviewed;         252 AA.
AC   A3N2M5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            EC=2.7.7.38 {ECO:0000255|HAMAP-Rule:MF_00057};
DE   AltName: Full=CMP-2-keto-3-deoxyoctulosonic acid synthase 2 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CKS 2 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CMP-KDO synthase 2 {ECO:0000255|HAMAP-Rule:MF_00057};
GN   Name=kdsB2 {ECO:0000255|HAMAP-Rule:MF_00057}; OrderedLocusNames=APL_1577;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
CC   -!- FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation
CC       into bacterial lipopolysaccharide in Gram-negative bacteria.
CC       {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deoxy-alpha-D-manno-oct-2-ulosonate + CTP = CMP-3-deoxy-
CC         beta-D-manno-octulosonate + diphosphate; Xref=Rhea:RHEA:23448,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:85986,
CC         ChEBI:CHEBI:85987; EC=2.7.7.38; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00057};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-
CC       octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-
CC       deoxy-D-manno-octulosonate and CTP: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00057}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00057}.
CC   -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00057}.
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DR   EMBL; CP000569; ABN74661.1; -; Genomic_DNA.
DR   RefSeq; WP_009874575.1; NC_009053.1.
DR   AlphaFoldDB; A3N2M5; -.
DR   SMR; A3N2M5; -.
DR   STRING; 416269.APL_1577; -.
DR   EnsemblBacteria; ABN74661; ABN74661; APL_1577.
DR   KEGG; apl:APL_1577; -.
DR   PATRIC; fig|416269.6.peg.1643; -.
DR   eggNOG; COG1212; Bacteria.
DR   HOGENOM; CLU_065038_1_0_6; -.
DR   OMA; VMMETET; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000001432; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033468; P:CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02517; CMP-KDO-Synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00057; KdsB; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR004528; KdsB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00466; kdsB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipopolysaccharide biosynthesis; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..252
FT                   /note="3-deoxy-manno-octulosonate cytidylyltransferase 2"
FT                   /id="PRO_0000369990"
SQ   SEQUENCE   252 AA;  28530 MW;  7415A4317C328B94 CRC64;
     MKFTIIIPAR YASTRLPRKP LLDILGKPMI QHVWERAKQA GGHRVIIATD HSEIAEVVTR
     FGGEVCLTSD KHSSGTERLA EVVSKMNISD DEIIVNVQGD EPLIPPCIIK QVAENLDNHQ
     VNMATLAVKL TQRDELFNPN VVKVLSDKNG MALYFSRAAI PFARDNFPDC SDDFVTQNQY
     LRHIGIYAYR AGFIKQYVQW QPTALEQLES LEQLRALWNG EKIHLDIALE TPEVGVDTQE
     DLERVRLILS NK