KPSU5_ECOLX
ID KPSU5_ECOLX Reviewed; 246 AA.
AC P42216;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 127.
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=kpsU;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K5;
RX PubMed=8397187; DOI=10.1128/jb.175.18.5978-5983.1993;
RA Pazzani C., Rosenow C., Boulnois G.J., Bronner D., Jann K., Roberts I.S.;
RT "Molecular analysis of region 1 of the Escherichia coli K5 antigen gene
RT cluster: a region encoding proteins involved in cell surface expression of
RT capsular polysaccharide.";
RL J. Bacteriol. 175:5978-5983(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7875563; DOI=10.1111/j.1574-6968.1995.tb07352.x;
RA Rosenow C., Roberts I.S., Jann K.;
RT "Isolation from recombinant Escherichia coli and characterization of CMP-
RT Kdo synthetase, involved in the expression of the capsular K5
RT polysaccharide (K-CKS).";
RL FEMS Microbiol. Lett. 125:159-164(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=8706906; DOI=10.1016/0014-5793(96)00724-7;
RA Jelakovic S., Jann K., Schulz G.E.;
RT "The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-
RT manno-octonic acid synthetase from Escherichia coli.";
RL FEBS Lett. 391:157-161(1996).
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.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00057}.
CC -!- SIMILARITY: Belongs to the KdsB family. {ECO:0000255|HAMAP-
CC Rule:MF_00057}.
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; X74567; CAA52657.1; -; Genomic_DNA.
DR EMBL; S76943; AAB33584.1; -; Genomic_DNA.
DR PIR; C48492; C48492.
DR RefSeq; WP_000030749.1; NZ_WWEL01000034.1.
DR PDB; 1GQ9; X-ray; 2.60 A; A/B=2-246.
DR PDB; 1GQC; X-ray; 2.60 A; A/B=2-246.
DR PDB; 1H6J; X-ray; 2.32 A; A/B=2-246.
DR PDB; 1H7E; X-ray; 1.83 A; A/B=2-246.
DR PDB; 1H7F; X-ray; 2.12 A; A/B=2-246.
DR PDB; 1H7G; X-ray; 2.13 A; A/B=2-246.
DR PDB; 1H7H; X-ray; 2.30 A; A/B=2-246.
DR PDB; 1H7T; X-ray; 2.48 A; A/B=2-246.
DR PDBsum; 1GQ9; -.
DR PDBsum; 1GQC; -.
DR PDBsum; 1H6J; -.
DR PDBsum; 1H7E; -.
DR PDBsum; 1H7F; -.
DR PDBsum; 1H7G; -.
DR PDBsum; 1H7H; -.
DR PDBsum; 1H7T; -.
DR AlphaFoldDB; P42216; -.
DR SMR; P42216; -.
DR DrugBank; DB04482; Cmp-2-Keto-3-Deoxy-Octulosonic Acid.
DR DrugBank; DB04555; Cytidine-5'-Diphosphate.
DR DrugBank; DB03403; Cytidine-5'-Monophosphate.
DR DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR PRIDE; P42216; -.
DR OMA; MSIKEHE; -.
DR OrthoDB; 1345588at2; -.
DR BRENDA; 2.7.7.38; 2026.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00358; UER00476.
DR EvolutionaryTrace; P42216; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis;
KW Nucleotidyltransferase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..246
FT /note="3-deoxy-manno-octulosonate cytidylyltransferase"
FT /id="PRO_0000188523"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1GQC"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1H7E"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1H7E"
FT HELIX 228..244
FT /evidence="ECO:0007829|PDB:1H7E"
SQ SEQUENCE 246 AA; 27159 MW; 3D8946D30799E6BB CRC64;
MSKAVIVIPA RYGSSRLPGK PLLDIVGKPM IQHVYERALQ VAGVAEVWVA TDDPRVEQAV
QAFGGKAIMT RNDHESGTDR LVEVMHKVEA DIYINLQGDE PMIRPRDVET LLQGMRDDPA
LPVATLCHAI SAAEAAEPST VKVVVNTRQD ALYFSRSPIP YPRNAEKARY LKHVGIYAYR
RDVLQNYSQL PESMPEQAES LEQLRLMNAG INIRTFEVAA TGPGVDTPAC LEKVRALMAQ
ELAENA
