ID CLPC1_MYCTU Reviewed; 848 AA.
AC P9WPC9; L0TD96; O06286; P0A522;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC1;
GN Name=clpC1; OrderedLocusNames=Rv3596c; ORFNames=MTCY07H7B.26;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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, INTERACTION WITH RSEA, AND DISRUPTION PHENOTYPE.
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.m111.011445;
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).
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-E
CC factor RseA in the presence of ClpP2. {ECO:0000250,
CC ECO:0000269|PubMed:20025669}.
CC -!- INTERACTION:
CC P9WPC9; P9WNK5: esxB; NbExp=3; IntAct=EBI-1254029, EBI-1253936;
CC -!- DISRUPTION PHENOTYPE: Depletion experiments (using anti-sense RNA)
CC stops degradation of anti-sigma-E factor RseA.
CC {ECO:0000269|PubMed:20025669}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46419.1; -; Genomic_DNA.
DR PIR; E70954; E70954.
DR RefSeq; WP_003419511.1; NZ_NVQJ01000056.1.
DR RefSeq; YP_177995.1; NC_000962.3.
DR PDB; 3WDB; X-ray; 1.37 A; A=1-145.
DR PDB; 3WDC; X-ray; 1.18 A; A=1-145.
DR PDB; 3WDD; X-ray; 1.18 A; A=3-145.
DR PDB; 3WDE; X-ray; 1.44 A; A=1-145.
DR PDB; 6CN8; X-ray; 1.40 A; A=1-145.
DR PDB; 6PBA; X-ray; 1.77 A; A=1-145.
DR PDB; 6PBQ; X-ray; 1.60 A; A=1-145.
DR PDB; 6PBS; X-ray; 2.50 A; A/B/C/G/I/K/M/O/T/W/Y/e=1-145.
DR PDB; 6UCR; X-ray; 2.30 A; A=1-145.
DR PDB; 7AA4; X-ray; 1.68 A; A=1-148.
DR PDB; 8A8U; EM; 3.62 A; A/B/C/D/E/F=1-848.
DR PDB; 8A8V; EM; 3.34 A; A/B/C/D/E/F=1-848.
DR PDB; 8A8W; EM; 4.29 A; A/B/C/D/E/F=1-848.
DR PDB; 8B9U; X-ray; 2.25 A; A/B=1-144.
DR PDBsum; 3WDB; -.
DR PDBsum; 3WDC; -.
DR PDBsum; 3WDD; -.
DR PDBsum; 3WDE; -.
DR PDBsum; 6CN8; -.
DR PDBsum; 6PBA; -.
DR PDBsum; 6PBQ; -.
DR PDBsum; 6PBS; -.
DR PDBsum; 6UCR; -.
DR PDBsum; 7AA4; -.
DR PDBsum; 8A8U; -.
DR PDBsum; 8A8V; -.
DR PDBsum; 8A8W; -.
DR PDBsum; 8B9U; -.
DR AlphaFoldDB; P9WPC9; -.
DR EMDB; EMD-15240; -.
DR EMDB; EMD-15241; -.
DR EMDB; EMD-15242; -.
DR SASBDB; P9WPC9; -.
DR SMR; P9WPC9; -.
DR DIP; DIP-61228N; -.
DR IntAct; P9WPC9; 3.
DR STRING; 83332.Rv3596c; -.
DR BindingDB; P9WPC9; -.
DR ChEMBL; CHEMBL4630874; -.
DR PaxDb; 83332-Rv3596c; -.
DR GeneID; 45427583; -.
DR GeneID; 885104; -.
DR KEGG; mtu:Rv3596c; -.
DR TubercuList; Rv3596c; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; P9WPC9; -.
DR OrthoDB; 9803641at2; -.
DR PhylomeDB; P9WPC9; -.
DR BRENDA; 3.4.21.92; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0044183; F:protein folding chaperone; IMP:MTBBASE.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..848
FT /note="ATP-dependent Clp protease ATP-binding subunit
FT ClpC1"
FT /id="PRO_0000191236"
FT DOMAIN 2..144
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT DOMAIN 425..460
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 5..70
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 80..144
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 171..418
FT /note="I"
FT REGION 479..670
FT /note="II"
FT REGION 821..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 553..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:3WDC"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:3WDC"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:3WDC"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:3WDC"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:3WDC"
FT TURN 169..174
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:8A8V"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:8A8V"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 352..370
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 376..389
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 397..414
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 503..508
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 522..536
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 546..553
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 559..571
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 588..594
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 632..644
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 690..704
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 707..712
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 715..718
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 724..742
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 743..745
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 753..763
FT /evidence="ECO:0007829|PDB:8A8V"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 773..779
FT /evidence="ECO:0007829|PDB:8A8V"
FT HELIX 782..790
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 799..804
FT /evidence="ECO:0007829|PDB:8A8V"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:8A8V"
SQ SEQUENCE 848 AA; 93552 MW; 4D536FBDA183CD94 CRC64;
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKSLE SLGISLEGVR
SQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
AQVLVKLGAE LTRVRQQVIQ LLSGYQGKEA AEAGTGGRGG ESGSPSTSLV LDQFGRNLTA
AAMEGKLDPV IGREKEIERV MQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QAIVHGEVPE
TLKDKQLYTL DLGSLVAGSR YRGDFEERLK KVLKEINTRG DIILFIDELH TLVGAGAAEG
AIDAASILKP KLARGELQTI GATTLDEYRK YIEKDAALER RFQPVQVGEP TVEHTIEILK
GLRDRYEAHH RVSITDAAMV AAATLADRYI NDRFLPDKAI DLIDEAGARM RIRRMTAPPD
LREFDEKIAE ARREKESAID AQDFEKAASL RDREKTLVAQ RAEREKQWRS GDLDVVAEVD
DEQIAEVLGN WTGIPVFKLT EAETTRLLRM EEELHKRIIG QEDAVKAVSK AIRRTRAGLK
DPKRPSGSFI FAGPSGVGKT ELSKALANFL FGDDDALIQI DMGEFHDRFT ASRLFGAPPG
YVGYEEGGQL TEKVRRKPFS VVLFDEIEKA HQEIYNSLLQ VLEDGRLTDG QGRTVDFKNT
VLIFTSNLGT SDISKPVGLG FSKGGGENDY ERMKQKVNDE LKKHFRPEFL NRIDDIIVFH
QLTREEIIRM VDLMISRVAG QLKSKDMALV LTDAAKALLA KRGFDPVLGA RPLRRTIQRE
IEDQLSEKIL FEEVGPGQVV TVDVDNWDGE GPGEDAVFTF TGTRKPPAEP DLAKAGAHSA
GGPEPAAR
//
