CLPP_CAUVN
ID CLPP_CAUVN Reviewed; 209 AA.
AC B8GX16; O87706;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=CCNA_02041;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-106.
RC STRAIN=NA1000 / CB15N;
RX PubMed=9755166; DOI=10.1093/emboj/17.19.5658;
RA Jenal U., Fuchs T.;
RT "An essential protease involved in bacterial cell-cycle control.";
RL EMBO J. 17:5658-5669(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24239291; DOI=10.1016/j.molcel.2013.10.014;
RA Aakre C.D., Phung T.N., Huang D., Laub M.T.;
RT "A bacterial toxin inhibits DNA replication elongation through a direct
RT interaction with the beta sliding clamp.";
RL Mol. Cell 52:617-628(2013).
CC -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC requires ATP hydrolysis. Has a chymotrypsin-like activity (By
CC similarity). Plays a major role in the degradation of misfolded
CC proteins (By similarity). Required for degradation of response
CC regulator CtrA, thus contributing to the G1-to-S transition
CC (PubMed:9755166). Required to degrade DNA replication inhibitor toxin
CC SocB, this function is probably the reason why the protease is
CC essential in this organism (PubMed:24239291). {ECO:0000255|HAMAP-
CC Rule:MF_00444, ECO:0000269|PubMed:24239291,
CC ECO:0000269|PubMed:9755166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC stack back to back to give a disk-like structure with a central cavity,
CC resembling the structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted (PubMed:9755166,
CC PubMed:24239291). When depleted for ClpP cells arrest before the
CC initiation of chromosome replication and are blocked in the cell
CC division process (PubMed:9755166). Deletion of socB permits slower than
CC wild-type growth of the clpP disruption. {ECO:0000269|PubMed:24239291,
CC ECO:0000269|PubMed:9755166}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACL95506.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA09090.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ010321; CAA09090.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001340; ACL95506.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_002517414.1; NC_011916.1.
DR AlphaFoldDB; B8GX16; -.
DR SMR; B8GX16; -.
DR MEROPS; S14.001; -.
DR PRIDE; B8GX16; -.
DR EnsemblBacteria; ACL95506; ACL95506; CCNA_02041.
DR GeneID; 7333372; -.
DR KEGG; ccs:CCNA_02041; -.
DR PATRIC; fig|565050.3.peg.1999; -.
DR HOGENOM; CLU_058707_3_2_5; -.
DR OMA; RDYWMKA; -.
DR OrthoDB; 1728970at2; -.
DR PhylomeDB; B8GX16; -.
DR BRENDA; 3.4.21.92; 1218.
DR PRO; PR:B8GX16; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..209
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000378281"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 131
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT MUTAGEN 106
FT /note="S->A: No longer rescues a chromosomal deletion of
FT clpP."
FT /evidence="ECO:0000269|PubMed:9755166"
SQ SEQUENCE 209 AA; 22989 MW; A8C7A7FF5050F845 CRC64;
MYDPVSTAMN LVPMVVEQTS RGERAFDIFS RLLKERIIFL TGPVEDGMAS LICAQLLFLE
SENPKKEIAM YINSPGGVVT AGLAIYDTMQ YIKSPVSTVC MGMAASMGSL LLAAGAAGQR
ISLPNARIMV HQPSGGFRGQ ASDIERHAED IIKTKRRLNE IYVKHCGRTY EEVERTLDRD
HFMSADEAKA WGLVDHVYDS RDAAEAGAE
