ID   CLPP1_RHOBA             Reviewed;         227 AA.
AC   Q7UK67;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit 1;
DE            EC=3.4.21.92;
DE   AltName: Full=Endopeptidase Clp 1;
GN   Name=clpP1; OrderedLocusNames=RB10826;
OS   Rhodopirellula baltica.
OC   Bacteria; Planctomycetes; Planctomycetacia; Planctomycetales;
OC   Planctomycetaceae; Pirellula.
OX   NCBI_TaxID=117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1;
RX   MEDLINE=22735913; PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T.,
RA   Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R.,
RA   Schlesner H., Amann R., Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp.
RT   strain 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294152; CAD77014.1; -; Genomic_DNA.
DR   RefSeq; NP_869636.1; -.
DR   GeneID; 1791253; -.
DR   GenomeReviews; BX119912_GR; RB10826.
DR   KEGG; rba:RB10826; -.
DR   NMPDR; fig|243090.1.peg.5976; -.
DR   HOGENOM; Q7UK67; -.
DR   OMA; Q7UK67; AREMINI.
DR   BioCyc; PSP117:RB10826-MON; -.
DR   BRENDA; 3.4.21.92; 280490.
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; -; 1.
DR   InterPro; IPR001907; Pept_S14_ClpP.
DR   InterPro; IPR018215; Pept_S14_ClpP_CS.
DR   PANTHER; PTHR10381; Pept_S14_ClpP; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR   PROSITE; PS00381; CLP_PROTEASE_SER; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease.
FT   CHAIN         1    227       ATP-dependent Clp protease proteolytic
FT                                subunit 1.
FT                                /FTId=PRO_0000179636.
FT   ACT_SITE    124    124       By similarity.
FT   ACT_SITE    149    149       By similarity.
SQ   SEQUENCE   227 AA;  25139 MW;  16CA525C877762AD CRC64;
     MSDPFGSPFP SLHDQNLNAQ HAMASDHRLA NAASYQSYQR QRQMTLGDLL LENRIVFMQG
     EIHYANANEI VMKLLYLQSE NRRKDIHLYI NSPGGSVTAT LAIYDTMQML SCPVATYCVG
     EACSGAAVLL IGGAKGKRFC LPNSRVMMHQ PLGGVSGQVS DIEIQAAEMF RYRDKLNEII
     SSHCGKSVEQ IAKDTDRDFF LDAQQAKEYG LVDDLLLGTP ASEEDED
//