CLPP2_MYCTU
ID CLPP2_MYCTU Reviewed; 214 AA.
AC P9WPC3; L0TCE9; O53187; P63783;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
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}; OrderedLocusNames=Rv2460c;
GN ORFNames=MTV008.16c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A PROTEASE, AND INTERACTION WITH RSEA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
RA Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
RT "RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis,
RT is inactivated by phosphorylation-dependent ClpC1P2 proteolysis.";
RL Mol. Microbiol. 75:592-606(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION AS A PROTEASE, AND INTERACTION WITH CLPP1 AND CLPX.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23314154; DOI=10.1093/nar/gks1468;
RA Jaiswal R.K., Prabha T.S., Manjeera G., Gopal B.;
RT "Mycobacterium tuberculosis RsdA provides a conformational rationale for
RT selective regulation of sigma-factor activity by proteolysis.";
RL Nucleic Acids Res. 41:3414-3423(2013).
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 similarity).
CC Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1
CC and ClpX. Degrades anti-sigma-E factor RseA in the presence of ClpC1.
CC Does not seem to act on anti-sigma-L factor RslA. {ECO:0000255|HAMAP-
CC Rule:MF_00444, ECO:0000269|PubMed:20025669,
CC ECO:0000269|PubMed:23314154}.
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 (By similarity).
CC Forms a complex with ClpP1 and ClpX. {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
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DR EMBL; AL123456; CCP45253.1; -; Genomic_DNA.
DR PIR; C70865; C70865.
DR RefSeq; NP_216976.1; NC_000962.3.
DR RefSeq; WP_003412648.1; NZ_NVQJ01000024.1.
DR PDB; 4U0G; X-ray; 3.20 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=13-214.
DR PDB; 5DZK; X-ray; 3.07 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=1-214.
DR PDB; 5E0S; X-ray; 2.90 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=1-214.
DR PDB; 6VGK; EM; 3.10 A; A/B/C/D/E/F/G=16-214.
DR PDB; 6VGN; EM; 3.10 A; A/B/C/D/E/F/G=15-214.
DR PDB; 6VGQ; EM; 3.50 A; A/B/C/D/E/F/G=15-214.
DR PDBsum; 4U0G; -.
DR PDBsum; 5DZK; -.
DR PDBsum; 5E0S; -.
DR PDBsum; 6VGK; -.
DR PDBsum; 6VGN; -.
DR PDBsum; 6VGQ; -.
DR AlphaFoldDB; P9WPC3; -.
DR SMR; P9WPC3; -.
DR IntAct; P9WPC3; 1.
DR STRING; 83332.Rv2460c; -.
DR ChEMBL; CHEMBL4662931; -.
DR PaxDb; P9WPC3; -.
DR DNASU; 888174; -.
DR GeneID; 888174; -.
DR KEGG; mtu:Rv2460c; -.
DR TubercuList; Rv2460c; -.
DR eggNOG; COG0740; Bacteria.
DR OMA; GFKRQDP; -.
DR PhylomeDB; P9WPC3; -.
DR BRENDA; 3.4.21.92; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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 3D-structure; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..214
FT /note="ATP-dependent Clp protease proteolytic subunit 2"
FT /id="PRO_0000179597"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5DZK"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 147..172
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:5E0S"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6VGK"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:5E0S"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5E0S"
SQ SEQUENCE 214 AA; 23540 MW; 4B26A854F0F984AB CRC64;
MNSQNSQIQP QARYILPSFI EHSSFGVKES NPYNKLFEER IIFLGVQVDD ASANDIMAQL
LVLESLDPDR DITMYINSPG GGFTSLMAIY DTMQYVRADI QTVCLGQAAS AAAVLLAAGT
PGKRMALPNA RVLIHQPSLS GVIQGQFSDL EIQAAEIERM RTLMETTLAR HTGKDAGVIR
KDTDRDKILT AEEAKDYGII DTVLEYRKLS AQTA
