CLPP1_MYCTU
ID CLPP1_MYCTU Reviewed; 200 AA.
AC P9WPC5; L0TBA3; O53188; P0A526;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp 1 {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP1 {ECO:0000255|HAMAP-Rule:MF_00444}; Synonyms=clpP;
GN OrderedLocusNames=Rv2461c; ORFNames=MTV008.17c;
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 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 [3]
RP FUNCTION AS A PROTEASE, AND SUBUNIT.
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17242518; DOI=10.1107/s0907444906050530;
RA Ingvarsson H., Mate M.J., Hogbom M., Portnoi D., Benaroudj N., Alzari P.M.,
RA Ortiz-Lombardia M., Unge T.;
RT "Insights into the inter-ring plasticity of caseinolytic proteases from the
RT X-ray structure of Mycobacterium tuberculosis ClpP1.";
RL Acta Crystallogr. D 63:249-259(2007).
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
CC ClpP2 and ClpX. Does not seem to act on anti-sigma-L factor (rslA).
CC {ECO:0000255|HAMAP-Rule:MF_00444, 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. Forms a complex
CC with ClpP2 and ClpX. {ECO:0000255|HAMAP-Rule:MF_00444,
CC ECO:0000269|PubMed:17242518, ECO:0000269|PubMed:23314154}.
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; CCP45254.1; -; Genomic_DNA.
DR PIR; D70865; D70865.
DR RefSeq; WP_003412650.1; NZ_NVQJ01000024.1.
DR RefSeq; YP_177883.1; NC_000962.3.
DR PDB; 2C8T; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-200.
DR PDB; 2CBY; X-ray; 2.60 A; A/B/C/D/E/F/G=1-200.
DR PDB; 2CE3; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-200.
DR PDB; 4U0G; X-ray; 3.20 A; H/I/J/K/L/M/N/V/W/X/Y/Z/a/b=7-200.
DR PDB; 4U0H; X-ray; 3.25 A; A/B/C/D/E/F/G=7-200.
DR PDB; 5DZK; X-ray; 3.07 A; H/I/J/K/L/M/N/h/i/j/k/l/m/n=1-200.
DR PDB; 5E0S; X-ray; 2.90 A; H/I/J/K/L/M/N/h/i/j/k/l/m/n=1-200.
DR PDB; 6VGK; EM; 3.10 A; H/I/J/K/L/M/N=7-200.
DR PDB; 6VGN; EM; 3.10 A; H/I/J/K/L/M/N=7-200.
DR PDB; 6VGQ; EM; 3.50 A; H/I/J/K/L/M/N=7-200.
DR PDBsum; 2C8T; -.
DR PDBsum; 2CBY; -.
DR PDBsum; 2CE3; -.
DR PDBsum; 4U0G; -.
DR PDBsum; 4U0H; -.
DR PDBsum; 5DZK; -.
DR PDBsum; 5E0S; -.
DR PDBsum; 6VGK; -.
DR PDBsum; 6VGN; -.
DR PDBsum; 6VGQ; -.
DR AlphaFoldDB; P9WPC5; -.
DR SMR; P9WPC5; -.
DR STRING; 83332.Rv2461c; -.
DR ChEMBL; CHEMBL4662931; -.
DR MEROPS; S14.008; -.
DR PaxDb; P9WPC5; -.
DR DNASU; 888176; -.
DR GeneID; 45426451; -.
DR GeneID; 888176; -.
DR KEGG; mtu:Rv2461c; -.
DR PATRIC; fig|83332.111.peg.2755; -.
DR TubercuList; Rv2461c; -.
DR eggNOG; COG0740; Bacteria.
DR OMA; RDYWMKA; -.
DR PhylomeDB; P9WPC5; -.
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: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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..200
FT /note="ATP-dependent Clp protease proteolytic subunit 1"
FT /id="PRO_0000179596"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:2CBY"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2CBY"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2CBY"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2CE3"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:2CBY"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5E0S"
FT HELIX 137..158
FT /evidence="ECO:0007829|PDB:2CBY"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2CBY"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2CBY"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2CBY"
SQ SEQUENCE 200 AA; 21708 MW; 2FDF6B71DE206953 CRC64;
MSQVTDMRSN SQGLSLTDSV YERLLSERII FLGSEVNDEI ANRLCAQILL LAAEDASKDI
SLYINSPGGS ISAGMAIYDT MVLAPCDIAT YAMGMAASMG EFLLAAGTKG KRYALPHARI
LMHQPLGGVT GSAADIAIQA EQFAVIKKEM FRLNAEFTGQ PIERIEADSD RDRWFTAAEA
LEYGFVDHII TRAHVNGEAQ
