P0A4I7 (CUTS_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sensor protein CutS
EC=2.7.13.3

Gene names

Name:	cutS
Ordered Locus Names:	SCO5863
ORF Names:	SC2E9.04

Organism

Streptomyces coelicolor

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Two-component regulatory system
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 414	414	Sensor protein CutS		PRO_0000074744
Regions
	Transmembrane	37 – 57	21	Helical; Potential
	Transmembrane	121 – 141	21	Helical; Potential
	Domain	142 – 194	53	HAMP
	Domain	202 – 414	213	Histidine kinase
Amino acid modifications
	Modified residue	205	1	Phosphohistidine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A4I7 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: B1CBC2DFBD0ABB4D	FASTA	414	44,496
	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

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL939125 Genomic DNA. Translation: CAA16472.1.
PIR	T34815.
RefSeq	NP_629985.1. NC_003888.3.
3D structure databases
ProteinModelPortal	P0A4I7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1101305.
GenomeReviews	Gene locus SCO5863 in contig AL645882_GR.
KEGG	sco:SCO5863.
NMPDR	fig|100226.1.peg.5812.
PATRIC	23741630. VBIStrCoe124346_5962.
Phylogenomic databases
HOGENOM	HBG334875.
OMA	PTIRIRL.
PhylomeDB	P0A4I7.
ProtClustDB	CLSK902991.
Family and domain databases
InterPro	IPR003594. 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]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
KO	K00936.
Pfam	PF00672. HAMP. 1 hit. PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM00304. HAMP. 1 hit. SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF47384. His_kin_homodim. 1 hit.
PROSITE	PS50885. HAMP. 1 hit. PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CUTS_STRCO

Accession

Primary (citable) accession number: P0A4I7
Secondary accession number(s): Q03757

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program