ID CLPP2_MYXXD Reviewed; 203 AA.
AC O30612; Q1CYG1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 01-MAY-2013, entry version 80.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 2;
DE EC=3.4.21.92;
DE AltName: Full=Endopeptidase Clp 2;
GN Name=clpP2; Synonyms=clpP; OrderedLocusNames=MXAN_6438;
OS Myxococcus xanthus (strain DK 1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Salmi D., Creighton C., Youderian P.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK 1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC major role in the degradation of misfolded proteins (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
CC the presence of ATP and magnesium. Alpha-casein is the usual test
CC substrate. In the absence of ATP, only oligopeptides shorter than
CC five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
CC and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu-
CC and -Tyr-|-Trp bonds also occurs).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S14 family.
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DR EMBL; AF013216; AAB97819.1; -; Genomic_DNA.
DR EMBL; CP000113; ABF86796.1; -; Genomic_DNA.
DR RefSeq; YP_634562.1; NC_008095.1.
DR ProteinModelPortal; O30612; -.
DR SMR; O30612; 3-189.
DR STRING; 246197.MXAN_6438; -.
DR MEROPS; S14.001; -.
DR EnsemblBacteria; ABF86796; ABF86796; MXAN_6438.
DR GeneID; 4103420; -.
DR KEGG; mxa:MXAN_6438; -.
DR PATRIC; 22655379; VBIMyxXan43560_6333.
DR eggNOG; COG0740; -.
DR HOGENOM; HOG000285833; -.
DR KO; K01358; -.
DR OMA; GHTIERI; -.
DR ProtClustDB; PRK00277; -.
DR BioCyc; MXAN246197:GIWU-6387-MONOMER; -.
DR BRENDA; 3.4.21.92; 6741.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:HAMAP.
DR HAMAP; MF_00444; ClpP; 1; -.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR018215; ClpP_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR TIGRFAMs; TIGR00493; clpP; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Protease; Serine protease.
FT CHAIN 1 203 ATP-dependent Clp protease proteolytic
FT subunit 2.
FT /FTId=PRO_0000179598.
FT ACT_SITE 97 97 By similarity.
FT ACT_SITE 122 122 By similarity.
SQ SEQUENCE 203 AA; 22327 MW; 6B2A23DE232C46AE CRC64;
MNVPFVIETT HRGERAYDLY SRLLKDRIIM LGTPVNDDVA NIIVAQLLFL ESEDPDKGIN
LYINSPGGSV TAGLAIYDTM QYVKCPVSTI CVGQAASMGA LLLLAGAKGK RYALPNSRIM
IHQPLGGAQG QATDIDIQAK EILRLRSYIN GLIVKHTGHT IERIEKDTER DYFMSAEDAR
QYGLIDEVVE KQRVIAPTPA PAK
//
