CLPX_MYCTU
ID CLPX_MYCTU Reviewed; 426 AA.
AC P9WPB9; L0T9P2; O53184; P0A528;
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 ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=Rv2457c;
GN ORFNames=MTV008.13c;
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 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, AND INTERACTION WITH CLPP1 AND CLPP2.
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: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP (By similarity). Degrades anti-sigma-D
CC factor RsdA when present in a complex with ClpP1 and ClpP2. Does not
CC seem to act on anti-sigma-L factor RslA. {ECO:0000255|HAMAP-
CC Rule:MF_00175, ECO:0000269|PubMed:23314154}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes (By similarity). Forms a complex
CC with ClpP1 and ClpP2. Interacts with RseA but does not seem to help
CC degrade it. {ECO:0000255|HAMAP-Rule:MF_00175,
CC ECO:0000269|PubMed:20025669, ECO:0000269|PubMed:23314154}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
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DR EMBL; AL123456; CCP45250.1; -; Genomic_DNA.
DR PIR; H70864; H70864.
DR RefSeq; NP_216973.1; NC_000962.3.
DR RefSeq; WP_003412634.1; NZ_NVQJ01000024.1.
DR AlphaFoldDB; P9WPB9; -.
DR SMR; P9WPB9; -.
DR STRING; 83332.Rv2457c; -.
DR PaxDb; P9WPB9; -.
DR DNASU; 888167; -.
DR GeneID; 45426447; -.
DR GeneID; 888167; -.
DR KEGG; mtu:Rv2457c; -.
DR TubercuList; Rv2457c; -.
DR eggNOG; COG1219; Bacteria.
DR OMA; HYKRVQA; -.
DR PhylomeDB; P9WPB9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IMP:CACAO.
DR GO; GO:0032272; P:negative regulation of protein polymerization; IDA:CACAO.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 1.
DR HAMAP; MF_00175; ClpX; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF06689; zf-C4_ClpX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..426
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_0000160388"
FT DOMAIN 1..54
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 426 AA; 46783 MW; B5C08194980F03D3 CRC64;
MARIGDGGDL LKCSFCGKSQ KQVKKLIAGP GVYICDECID LCNEIIEEEL ADADDVKLDE
LPKPAEIREF LEGYVIGQDT AKRTLAVAVY NHYKRIQAGE KGRDSRCEPV ELTKSNILML
GPTGCGKTYL AQTLAKMLNV PFAIADATAL TEAGYVGEDV ENILLKLIQA ADYDVKRAET
GIIYIDEVDK IARKSENPSI TRDVSGEGVQ QALLKILEGT QASVPPQGGR KHPHQEFIQI
DTTNVLFIVA GAFAGLEKII YERVGKRGLG FGAEVRSKAE IDTTDHFADV MPEDLIKFGL
IPEFIGRLPV VASVTNLDKE SLVKILSEPK NALVKQYIRL FEMDGVELEF TDDALEAIAD
QAIHRGTGAR GLRAIMEEVL LPVMYDIPSR DDVAKVVVTK ETVQDNVLPT IVPRKPSRSE
RRDKSA
