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P0A4I8 (CUTS_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sensor protein CutS

EC=2.7.13.3
Gene names
Name:cutS
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Member of the two-component regulatory system CutS/CutR, involved in the regulation of copper metabolism.

Catalytic activity

ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Contains 1 HAMP domain.

Contains 1 histidine kinase domain.

Ontologies

Keywords
   Biological processTwo-component regulatory system
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processpeptidyl-histidine phosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

two-component sensor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Sensor protein CutS
PRO_0000074745

Regions

Transmembrane37 – 5721Helical; Potential
Transmembrane121 – 14121Helical; Potential
Domain142 – 19453HAMP
Domain202 – 414213Histidine kinase

Amino acid modifications

Modified residue2051Phosphohistidine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A4I8 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: B1CBC2DFBD0ABB4D

FASTA41444,496
        10         20         30         40         50         60 
MATTPAPPGA PPKPTWDPRS ATPLPWLRPT IRIRLTLLYG GMFLIAGILL LSIIYLLAAQ 

        70         80         90        100        110        120 
AVRTGNEPLY KIVDFTDLKV SSSTCPVVDN GGLSLSDFNA AISDCMDHQR KVALDNLLSR 

       130        140        150        160        170        180 
SLLALLGLAV IAFAFGYAMA GRVLSPLGRI TRTARAVAGS DLSRRIELDG PDDELKELAD 

       190        200        210        220        230        240 
TFDDMLERLQ RAFTAQQRFV GNASHELRTP LAINRTLLEV HLSDPGAPVE LQQLGKTLLA 

       250        260        270        280        290        300 
TNERSELLVE GLLLLARSDN QIVERKPVDL AEVAGQAIDQ VHAEAESKGV EVRGTREAAV 

       310        320        330        340        350        360 
VQGNGVLLER IALNLVQNAV RYNVAGQGWV EVATAVENGQ AVLVVTNTGP VVPAYEVDNL 

       370        380        390        400        410 
FEPFRRLRTE RTGSDKGVGL GLSIARSVAR AHGGHISAQP REGGGLVMRV TLPV 

« Hide

References

[1]Chen C.W.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 66 / 1326.
[2]"A cloned ompR-like gene of Streptomyces lividans 66 suppresses defective melC1, a putative copper-transfer gene."
Tseng H.-C., Chen C.W.
Mol. Microbiol. 5:1187-1196(1991) [PubMed: 1956295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-190.
Strain: 66 / 1326.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58793 Genomic DNA. Translation: CAA41600.1.
PIRS15275.

3D structure databases

ProteinModelPortalP0A4I8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR003660. HAMP_linker_domain.
IPR004358. Sig_transdc_His_kin-like_C.
IPR003661. Sig_transdc_His_kin_sub1_dim/P.
IPR005467. Sig_transdc_His_kinase_core.
IPR009082. Sig_transdc_His_kinase_dimeric.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
PfamPF00672. HAMP. 1 hit.
PF02518. HATPase_c. 1 hit.
PF00512. HisKA. 1 hit.
[Graphical view]
PRINTSPR00344. BCTRLSENSOR.
SMARTSM00304. HAMP. 1 hit.
SM00387. HATPase_c. 1 hit.
SM00388. HisKA. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF47384. His_kin_homodim. 1 hit.
PROSITEPS50885. HAMP. 1 hit.
PS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCUTS_STRLI
AccessionPrimary (citable) accession number: P0A4I8
Secondary accession number(s): Q03757
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 31, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families