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Q56148 (CPT_STRVP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chloramphenicol 3-O phosphotransferase

Short name=CPT
EC=2.7.1.-
Gene names
Ordered Locus Names:SVEN_4064
OrganismStreptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745) [Complete proteome] [HAMAP]
Taxonomic identifier953739 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactivates chloramphenicol by catalyzing the transfer of the gamma-phosphate of ATP to the antibiotic's C-3' hydroxyl group.

Subunit structure

Homodimer.

Sequence similarities

To M.tuberculosis Rv2636.

Sequence caution

The sequence CCA57350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processAntibiotic resistance
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processresponse to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Chloramphenicol 3-O phosphotransferase
PRO_0000079295

Regions

Nucleotide binding10 – 178ATP

Sites

Active site371

Secondary structure

....................................... 178
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56148 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FC12D650A1C5D51A

FASTA17818,816
        10         20         30         40         50         60 
MTTRMIILNG GSSAGKSGIV RCLQSVLPEP WLAFGVDSLI EAMPLKMQSA EGGIEFDADG 

        70         80         90        100        110        120 
GVSIGPEFRA LEGAWAEGVV AMARAGARII IDDVFLGGAA AQERWRSFVG DLDVLWVGVR 

       130        140        150        160        170 
CDGAVAEGRE TARGDRVAGM AAKQAYVVHE GVEYDVEVDT THKESIECAW AIAAHVVP 

« Hide

References

« Hide 'large scale' references
[1]"Inactivation of chloramphenicol by O-phosphorylation. A novel resistance mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer."
Mosher R.H., Camp D.J., Yang K., Brown M.P., Shaw W.V., Vining L.C.
J. Biol. Chem. 270:27000-27006(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.
[2]"Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes."
Pullan S.T., Chandra G., Bibb M.J., Merrick M.
BMC Genomics 12:175-175(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.
[3]"The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism."
Izard T., Ellis J.
EMBO J. 19:2690-2700(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09991 Genomic DNA. Translation: AAB36569.1.
FR845719 Genomic DNA. Translation: CCA57350.1. Different initiation.
RefSeqYP_006879609.1. NC_018750.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GRQX-ray2.90A1-178[»]
1GRRX-ray2.90A1-178[»]
1QHNX-ray2.70A1-178[»]
1QHSX-ray2.80A1-178[»]
1QHXX-ray2.50A1-178[»]
1QHYX-ray2.60A1-178[»]
ProteinModelPortalQ56148.
SMRQ56148. Positions 1-178.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00446. Chloramphenicol.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCA57350; CCA57350; SVEN_4064.
GeneID13819222.
KEGGsve:SVEN_4064.

Organism-specific databases

CMRSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR012853. CPT.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF07931. CPT. 1 hit.
[Graphical view]
PIRSFPIRSF007531. CPT. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ56148.

Entry information

Entry nameCPT_STRVP
AccessionPrimary (citable) accession number: Q56148
Secondary accession number(s): F2RH22
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references