ID   CLPC1_MYCTO             Reviewed;         848 AA.
AC   P9WPC8; L0TD96; O06286; P0A522;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC1;
GN   Name=clpC1; OrderedLocusNames=MT3703;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   INDUCTION.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=19376862; DOI=10.1128/jb.00064-09;
RA   Mehra S., Kaushal D.;
RT   "Functional genomics reveals extended roles of the Mycobacterium
RT   tuberculosis stress response factor sigmaH.";
RL   J. Bacteriol. 191:3965-3980(2009).
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). {ECO:0000250}.
CC   -!- INDUCTION: Expression requires transcriptional regulator ClgR.
CC       {ECO:0000269|PubMed:19376862}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48060.1; -; Genomic_DNA.
DR   PIR; E70954; E70954.
DR   RefSeq; WP_010924687.1; NC_002755.2.
DR   AlphaFoldDB; P9WPC8; -.
DR   SMR; P9WPC8; -.
DR   EnsemblBacteria; AAK48060; AAK48060; MT3703.
DR   KEGG; mtc:MT3703; -.
DR   HOGENOM; CLU_005070_4_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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   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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Repeat.
FT   CHAIN           1..848
FT                   /note="ATP-dependent Clp protease ATP-binding subunit
FT                   ClpC1"
FT                   /id="PRO_0000426974"
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"
SQ   SEQUENCE   848 AA;  93524 MW;  4ECC545AD512BE83 CRC64;
     MFERFTDRAR KVVVLAQEEA 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