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ATP-dependent Clp protease proteolytic subunit 2 (EC 3.4.21.92) (Endopeptidase Clp 2)

 CLPP2_MYCTU             Reviewed;         214 AA.
P9WPC3; L0TCE9; O53187; P63783;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
23-MAY-2018, entry version 27.
RecName: Full=ATP-dependent Clp protease proteolytic subunit 2 {ECO:0000255|HAMAP-Rule:MF_00444};
EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
AltName: Full=Endopeptidase Clp 2 {ECO:0000255|HAMAP-Rule:MF_00444};
Name=clpP2 {ECO:0000255|HAMAP-Rule:MF_00444};
OrderedLocusNames=Rv2460c; ORFNames=MTV008.16c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION AS A PROTEASE, AND INTERACTION WITH RSEA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
"RseA, the SigE specific anti-sigma factor of Mycobacterium
tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2
proteolysis.";
Mol. Microbiol. 75:592-606(2010).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[4]
FUNCTION AS A PROTEASE, AND INTERACTION WITH CLPP1 AND CLPX.
STRAIN=ATCC 25618 / H37Rv;
PubMed=23314154; DOI=10.1093/nar/gks1468;
Jaiswal R.K., Prabha T.S., Manjeera G., Gopal B.;
"Mycobacterium tuberculosis RsdA provides a conformational rationale
for selective regulation of sigma-factor activity by proteolysis.";
Nucleic Acids Res. 41:3414-3423(2013).
-!- FUNCTION: Cleaves peptides in various proteins in a process that
requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
major role in the degradation of misfolded proteins (By
similarity). Degrades anti-sigma-D factor RsdA when present in a
complex with ClpP1 and ClpX. Degrades anti-sigma-E factor RseA in
the presence of ClpC1. Does not seem to act on anti-sigma-L factor
RslA. {ECO:0000255|HAMAP-Rule:MF_00444,
ECO:0000269|PubMed:20025669, ECO:0000269|PubMed:23314154}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in
the presence of ATP and magnesium. Alpha-casein is the usual test
substrate. In the absence of ATP, only oligopeptides shorter than
five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec;
and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-
Leu- and -Tyr-|-Trp bonds also occurs). {ECO:0000255|HAMAP-
Rule:MF_00444}.
-!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
which stack back to back to give a disk-like structure with a
central cavity, resembling the structure of eukaryotic proteasomes
(By similarity). Forms a complex with ClpP1 and ClpX.
{ECO:0000255|HAMAP-Rule:MF_00444}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
-!- SIMILARITY: Belongs to the peptidase S14 family.
{ECO:0000255|HAMAP-Rule:MF_00444}.
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EMBL; AL123456; CCP45253.1; -; Genomic_DNA.
PIR; C70865; C70865.
RefSeq; NP_216976.1; NC_000962.3.
RefSeq; WP_003412648.1; NZ_KK339370.1.
PDB; 4U0G; X-ray; 3.20 A; A/B/C/D/E/F/G/O/P/Q/R/S/T/U=13-214.
PDB; 5DZK; X-ray; 3.07 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=1-214.
PDB; 5E0S; X-ray; 2.90 A; A/B/C/D/E/F/G/a/b/c/d/e/f/g=1-214.
PDBsum; 4U0G; -.
PDBsum; 5DZK; -.
PDBsum; 5E0S; -.
ProteinModelPortal; P9WPC3; -.
SMR; P9WPC3; -.
IntAct; P9WPC3; 1.
STRING; 83332.Rv2460c; -.
PaxDb; P9WPC3; -.
PRIDE; P9WPC3; -.
EnsemblBacteria; CCP45253; CCP45253; Rv2460c.
GeneID; 888174; -.
KEGG; mtu:Rv2460c; -.
TubercuList; Rv2460c; -.
eggNOG; ENOG4105CCQ; Bacteria.
eggNOG; COG0740; LUCA.
KO; K01358; -.
OMA; GIFDTMQ; -.
PhylomeDB; P9WPC3; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0040007; P:growth; IMP:MTBBASE.
CDD; cd07017; S14_ClpP_2; 1.
HAMAP; MF_00444; ClpP; 1.
InterPro; IPR001907; ClpP.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR023562; ClpP/TepA.
InterPro; IPR033135; ClpP_His_AS.
InterPro; IPR018215; ClpP_Ser_AS.
PANTHER; PTHR10381; PTHR10381; 1.
Pfam; PF00574; CLP_protease; 1.
PRINTS; PR00127; CLPPROTEASEP.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PROSITE; PS00381; CLP_PROTEASE_SER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Hydrolase; Protease;
Reference proteome; Serine protease.
CHAIN 1 214 ATP-dependent Clp protease proteolytic
subunit 2.
/FTId=PRO_0000179597.
ACT_SITE 110 110 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_00444}.
ACT_SITE 135 135 {ECO:0000255|HAMAP-Rule:MF_00444}.
STRAND 19 23 {ECO:0000244|PDB:4U0G}.
STRAND 26 30 {ECO:0000244|PDB:4U0G}.
HELIX 32 38 {ECO:0000244|PDB:4U0G}.
STRAND 41 44 {ECO:0000244|PDB:4U0G}.
HELIX 50 66 {ECO:0000244|PDB:4U0G}.
STRAND 72 78 {ECO:0000244|PDB:4U0G}.
HELIX 83 95 {ECO:0000244|PDB:4U0G}.
STRAND 96 98 {ECO:0000244|PDB:4U0G}.
STRAND 100 109 {ECO:0000244|PDB:4U0G}.
HELIX 111 117 {ECO:0000244|PDB:4U0G}.
STRAND 124 126 {ECO:0000244|PDB:4U0G}.
STRAND 131 134 {ECO:0000244|PDB:4U0G}.
STRAND 138 146 {ECO:0000244|PDB:4U0G}.
HELIX 147 172 {ECO:0000244|PDB:4U0G}.
HELIX 176 183 {ECO:0000244|PDB:4U0G}.
STRAND 187 190 {ECO:0000244|PDB:4U0G}.
HELIX 191 197 {ECO:0000244|PDB:4U0G}.
STRAND 201 203 {ECO:0000244|PDB:4U0G}.
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


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