Q7W7F9 (KDSB_BORPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-deoxy-manno-octulosonate cytidylyltransferase
EC=2.7.7.38

Alternative name(s):
CMP-2-keto-3-deoxyoctulosonic acid synthase
Short name=CKS
Short name=CMP-KDO synthase

Gene names

Name:	kdsB
Ordered Locus Names:	BPP2561

Organism

Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253) [Complete proteome] [HAMAP]

Taxonomic identifier

257311 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella parapertussis

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria By similarity. HAMAP-Rule MF_00057
Catalytic activity	CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate. HAMAP-Rule MF_00057
Pathway	Nucleotide-sugar biosynthesis; CMP-3-deoxy-D-manno-octulosonate biosynthesis; CMP-3-deoxy-D-manno-octulosonate from 3-deoxy-D-manno-octulosonate and CTP: step 1/1. HAMAP-Rule MF_00057 Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. HAMAP-Rule MF_00057
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00057.
Sequence similarities	Belongs to the KdsB family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	CMP-keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway keto-3-deoxy-D-manno-octulosonic acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-deoxy-manno-octulosonate cytidylyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 254	254	3-deoxy-manno-octulosonate cytidylyltransferase HAMAP-Rule MF_00057		PRO_1000091861

Sequences

	Sequence		Length	Mass (Da)
	Q7W7F9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 7B31B80539954953	FASTA	254	27,060
	10 20 30 40 50 60 MSFTVLIPAR LASTRLPDKP LADIAGKPMV VRVAERAALS GAERVMIATD DARVQQAAAD 70 80 90 100 110 120 HGHAAILTRP DHPTGTDRLS EAVDALGLPD DAIVVNVQGD EPLIEPALID AVAAQLVAAP 130 140 150 160 170 180 HADIATCACP LADAEALFNP NVVKVVCAAD RRALYFSRAP IPWARDALAG GARVLAPGLP 190 200 210 220 230 240 AWHHIGIYAY RVAFLRRFPA LSQGQLERYE SLEQLRAMEH GHVIVVHHTD SAPAAGVDTP 250 ADLERARAAY TNRL

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640430 Genomic DNA. Translation: CAE37855.1.
RefSeq	NP_884789.1. NC_002928.3.
3D structure databases
HSSP	HSSP built from PDB template 1VH3 based on UniProtKB P44490.
ProteinModelPortal	Q7W7F9.
ModBase	Search...
Protein-protein interaction databases
STRING	257311.BPP2561.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE37855; CAE37855; BPP2561.
GeneID	1666232.
KEGG	bpa:BPP2561.
PATRIC	21149013. VBIBorPar43418_2687.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1212.
HOGENOM	HOG000007602.
KO	K00979.
OMA	NSGTERC.
ProtClustDB	PRK05450.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP2561-MONOMER.
UniPathway	UPA00030. UPA00358; UER00476.
Family and domain databases
HAMAP	MF_00057. CMP-KDO_synth.
InterPro	IPR003329. Cytidylyl_trans. IPR004528. KdsB. [Graphical view]
PANTHER	PTHR21485:SF4. PTHR21485:SF4. 1 hit.
Pfam	PF02348. CTP_transf_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00466. kdsB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KDSB_BORPA

Accession

Primary (citable) accession number: Q7W7F9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program