CLPC1_MYCTU
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 03-AUG-2022, entry version 50.
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; 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 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.m111.011627;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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 AlphaFoldDB; P9WPC9; -.
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; P9WPC9; -.
DR GeneID; 45427583; -.
DR GeneID; 885104; -.
DR KEGG; mtu:Rv3596c; -.
DR TubercuList; Rv3596c; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; ERMKAVM; -.
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 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 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"
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
