ID   CLPC1_MYCS2             Reviewed;         848 AA.
AC   A0R574;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC1;
GN   Name=clpC1; OrderedLocusNames=MSMEG_6091, MSMEI_5933;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
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).
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 (Probable). {ECO:0000250,
CC       ECO:0000269|PubMed:20025669, ECO:0000305}.
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; CP000480; ABK74692.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42366.1; -; Genomic_DNA.
DR   RefSeq; WP_011731031.1; NZ_SIJM01000046.1.
DR   RefSeq; YP_890312.1; NC_008596.1.
DR   AlphaFoldDB; A0R574; -.
DR   SMR; A0R574; -.
DR   STRING; 246196.MSMEI_5933; -.
DR   PRIDE; A0R574; -.
DR   EnsemblBacteria; ABK74692; ABK74692; MSMEG_6091.
DR   EnsemblBacteria; AFP42366; AFP42366; MSMEI_5933.
DR   GeneID; 66737376; -.
DR   KEGG; msg:MSMEI_5933; -.
DR   KEGG; msm:MSMEG_6091; -.
DR   PATRIC; fig|246196.19.peg.5930; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..848
FT                   /note="ATP-dependent Clp protease ATP-binding subunit
FT                   ClpC1"
FT                   /id="PRO_0000422952"
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          811..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         553..560
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         617..626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   848 AA;  93553 MW;  FBC77898B659DA99 CRC64;
     MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKSLE SLGISLEGVR
     SQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA
     AQVLVKLGAE LTRVRQQVIQ LLSGYQGKEA AEAGTGGRGG ESGNPSTSLV LDQFGRNLTA
     AAMEGKLDPV IGREKEIERV MQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QAIVHGEVPE
     TLKDKQLYTL DLGSLVAGSR YRGDFEERLK KVLKEINTRG DIILFIDELH TLVGAGAAEG
     AIDAASILKP KLARGELQTI GATTLDEYRK YIEKDAALER RFQPVQVGEP TVEHTIEILK
     GLRDRYEAHH RVSITDSAMV AAATLADRYI NDRFLPDKAI DLIDEAGARM RIRRMTAPPD
     LREFDEKIAD ARREKESAID AQDFEKAAAL RDKEKQLVAQ RAEREKQWRS GDLDVVAEVD
     DEQIAEVLGN WTGIPVFKLT EEETTRLLRM EEELHKRIIG QEDAVKAVSK AIRRTRAGLK
     DPKRPSGSFI FAGPSGVGKT ELSKALANFL FGDDDALIQI DMGEFHDRFT ASRLFGAPPG
     YVGYEEGGQL TEKVRRKPFS VVLFDEIEKA HQEIYNSLLQ VLEDGRLTDG QGRTVDFKNT
     VLIFTSNLGT SDISKAVGLG FSQGGSENNY ERMKQKVHDE LKKHFRPEFL NRIDDIIVFH
     QLTQDEIIQM VDLMIGRVSN QLKTKDMALE LSDKAKALLA KRGFDPVLGA RPLRRTIQRE
     IEDQLSEKIL FEEIGPGQLV TVDVEGWDGE GQGEDAKFTF SGGPKRAETA EPDLAGAGAA
     GAPTAGTE