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Database: UniProt
Entry: O30612
LinkDB: O30612
Original site: O30612 
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   29-OCT-2014, entry version 88.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 2 {ECO:0000255|HAMAP-Rule:MF_00444};
DE            EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp 2 {ECO:0000255|HAMAP-Rule:MF_00444};
GN   Name=clpP2 {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=clpP;
GN   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.
CC       {ECO:0000255|HAMAP-Rule:MF_00444}.
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). {ECO:0000255|HAMAP-
CC       Rule:MF_00444}.
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
CC       which stack back to back to give a disk-like structure with a
CC       central cavity, resembling the structure of eukaryotic
CC       proteasomes. {ECO:0000255|HAMAP-Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00444}.
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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   OrthoDB; EOG6Z3KQ0; -.
DR   BioCyc; MXAN246197:GIWU-6387-MONOMER; -.
DR   BRENDA; 3.4.21.92; 6741.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.226.10; -; 1.
DR   HAMAP; MF_00444; ClpP; 1.
DR   InterPro; IPR001907; ClpP.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
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   SUPFAM; SSF52096; SSF52096; 1.
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   Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN         1    203       ATP-dependent Clp protease proteolytic
FT                                subunit 2.
FT                                /FTId=PRO_0000179598.
FT   ACT_SITE     97     97       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00444}.
FT   ACT_SITE    122    122       {ECO:0000255|HAMAP-Rule:MF_00444}.
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
//
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