P63783 (CLPP2_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent Clp protease proteolytic subunit 2
EC=3.4.21.92

Alternative name(s):
Endopeptidase Clp 2

Gene names

Name:	clpP2
Ordered Locus Names:	Rv2460c, MT2535
ORF Names:	MTV008.16c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00444
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-Rule MF_00444
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00444.
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 Reference proteome
Gene Ontology (GO)
Biological_process	growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE proteolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE cytosol Inferred from direct assay PubMed 15525680. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352PubMed 15525680. Source: MTBBASE
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 – 214	214	ATP-dependent Clp protease proteolytic subunit 2 HAMAP-Rule MF_00444		PRO_0000179597
Sites
	Active site	110	1	By similarity
	Active site	135	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63783 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 4B26A854F0F984AB	FASTA	214	23,540
	10 20 30 40 50 60 MNSQNSQIQP QARYILPSFI EHSSFGVKES NPYNKLFEER IIFLGVQVDD ASANDIMAQL 70 80 90 100 110 120 LVLESLDPDR DITMYINSPG GGFTSLMAIY DTMQYVRADI QTVCLGQAAS AAAVLLAAGT 130 140 150 160 170 180 PGKRMALPNA RVLIHQPSLS GVIQGQFSDL EIQAAEIERM RTLMETTLAR HTGKDAGVIR 190 200 210 KDTDRDKILT AEEAKDYGII DTVLEYRKLS AQTA

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000516 Genomic DNA. Translation: AAK46835.1. AL123456 Genomic DNA. Translation: CCP45253.1.
PIR	C70865.
RefSeq	NP_216976.1. NC_000962.3. NP_337021.1. NC_002755.2. YP_006515897.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P63783.
SMR	P63783. Positions 33-204.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63783. 1 interaction.
STRING	83332.Rv2460c.
Protein family/group databases
MEROPS	S14.009.
Proteomic databases
PaxDb	P63783.
PRIDE	P63783.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK46835; AAK46835; MT2535.
GeneID	13319170. 888174. 925797.
KEGG	mtc:MT2535. mtu:Rv2460c.
PATRIC	18127328. VBIMycTub22151_2772.
Organism-specific databases
TubercuList	Rv2460c.
Phylogenomic databases
eggNOG	COG0740.
HOGENOM	HOG000285833.
KO	K01358.
OMA	IQGQVSD.
ProtClustDB	PRK12553.
Enzyme and pathway databases
BRENDA	3.4.21.92. 3445.
Family and domain databases
HAMAP	MF_00444. ClpP.
InterPro	IPR001907. ClpP. IPR023562. ClpP/TepA. IPR018215. ClpP_AS. [Graphical view]
PANTHER	PTHR10381. PTHR10381. 1 hit.
Pfam	PF00574. CLP_protease. 1 hit. [Graphical view]
PRINTS	PR00127. CLPPROTEASEP.
PROSITE	PS00382. CLP_PROTEASE_HIS. 1 hit. PS00381. CLP_PROTEASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLPP2_MYCTU

Accession

Primary (citable) accession number: P63783
Secondary accession number(s): L0TCE9, O53187

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 29, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program