ID   KDSB_CHLTR              Reviewed;         254 AA.
AC   P0CD75; O84185; Q59320;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CKS {ECO:0000255|HAMAP-Rule:MF_00057};
DE            Short=CMP-KDO synthase {ECO:0000255|HAMAP-Rule:MF_00057};
GN   Name=kdsB {ECO:0000255|HAMAP-Rule:MF_00057}; OrderedLocusNames=CT_182;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67774.1; -; Genomic_DNA.
DR   PIR; G71545; G71545.
DR   RefSeq; NP_219686.1; NC_000117.1.
DR   RefSeq; WP_009871528.1; NC_000117.1.
DR   AlphaFoldDB; P0CD75; -.
DR   SMR; P0CD75; -.
DR   STRING; 813.O172_00985; -.
DR   EnsemblBacteria; AAC67774; AAC67774; CT_182.
DR   GeneID; 884946; -.
DR   KEGG; ctr:CT_182; -.
DR   PATRIC; fig|272561.5.peg.196; -.
DR   HOGENOM; CLU_065038_0_1_0; -.
DR   InParanoid; P0CD75; -.
DR   OMA; FMATCAK; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00358; UER00476.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008690; F:3-deoxy-manno-octulosonate cytidylyltransferase activity; IBA:GO_Central.
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..254
FT                   /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT                   /id="PRO_0000188500"
SQ   SEQUENCE   254 AA;  28011 MW;  7F48F21C32950606 CRC64;
     MFAFLTSKKV GILPSRWGSS RFPGKPLAKI LGKTLVQRSY ENALSSQSLD CVVVATDDQR
     IFDHVVEFGG LCVMTSTSCA NGTERVEEVV SRHFPQAEIV VNIQGDEPCL SPTVIDGLVS
     TLENNPAADM VTSVTETTDP EAILTDHKVK CVFDKNGKAL YFSRSAIPHN FKHPTPIYLH
     IGVYAFRKAF LSEYVKIPPS SLSLAEDLEQ LRVLEIGRSI YVHVVQNATG PSVDYPEDIT
     KVEQYLLCLS KASF