Reviewed, UniProtKB/Swiss-Prot Q9F315 (CLPP1_STRCO)

Names and origin

Protein names

Recommended name:
    ATP-dependent Clp protease proteolytic subunit 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1

Gene names

Name:	clpP1
Ordered Locus Names:	SCO2619
ORF Names:	SCC80.04c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins By similarity.
Catalytic activity	Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). HAMAP MF_00444
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase S14 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase 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 – 219	219	ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444		PRO_0000179664
Sites
	Active site	113	1	By similarity
	Active site	138	1	By similarity
Experimental info
	Sequence conflict	125 – 127	3	GKR → RQ in AAC70947. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9F315-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 235A828E5B1E0BDD	FASTA	219	23,229
	10 20 30 40 50 60 MRRPGAVVRR AGGYVTNLMP SAAGEPSIGG GLGDQVYNRL LGERIIFLGQ PVDDDIANKI 70 80 90 100 110 120 TAQLLLLASD PDKDIFLYIN SPGGSITAGM AIYDTMQYIK NDVVTIAMGL AASMGQFLLS 130 140 150 160 170 180 AGTPGKRFAL PNAEILIHQP SAGLAGSASD IKIHAERLLH TKRRMAELTS QHTGQTIEQI 190 200 210 TRDSDRDRWF DAFEAKEYGL IDDVIATAAG MPGGGGTGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alteration of the synthesis of the Clp ATP-dependent protease affects morphological and physiological differentiation in Streptomyces." de Crecy-Lagard V., Servant-Moisson P., Viala J., Grandvalet C., Mazodier P. Mol. Microbiol. 32:505-517(1999) [PubMed: 10320574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.
[2]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF071885 Genomic DNA. Translation: AAC70947.1. AL939113 Genomic DNA. Translation: CAC09995.1.
RefSeq	NP_626855.1.
3D structure databases
HSSP	HSSP built from PDB template 1TYF based on UniProtKB P19245.
ModBase	Search...
Protein family/group databases
MEROPS	S14.008.
Genome annotation databases
GeneID	1098053.
GenomeReviews	Gene locus SCO2619 in contig AL645882_GR.
KEGG	sco:SCO2619.
NMPDR	fig|100226.1.peg.2584.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9F315.
OMA	DGVANSL.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO2619-MON.
BRENDA	3.4.21.92. 1084.
Family and domain databases
HAMAP	MF_00444. [Tree]
InterPro	IPR001907. Pept_S14_ClpP. IPR018215. Pept_S14_ClpP_AS. [Graphical view]
PANTHER	PTHR10381. Pept_S14_ClpP. 1 hit.
Pfam	PF00574. CLP_protease. 1 hit. [Graphical view]
PRINTS	PR00127. CLPPROTEASEP.
PROSITE	PS00382. CLP_PROTEASE_HIS. 1 hit. PS00381. CLP_PROTEASE_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLPP1_STRCO

Accession

Primary (citable) accession number: Q9F315
Secondary accession number(s): Q9ZH59

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)