ID A0A167WG22_9BURK Unreviewed; 913 AA.
AC A0A167WG22;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:ANB76497.1};
GN ORFNames=AYM40_30280 {ECO:0000313|EMBL:ANB76497.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB76497.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB76497.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB76497.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP014579; ANB76497.1; -; Genomic_DNA.
DR RefSeq; WP_063499720.1; NZ_CP014579.1.
DR AlphaFoldDB; A0A167WG22; -.
DR STRING; 1804984.AYM40_30280; -.
DR KEGG; buz:AYM40_30280; -.
DR Proteomes; UP000076852; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA_B PROTEASE ATP BINDING SUBUNIT-RELATED; 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; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Hydrolase {ECO:0000313|EMBL:ANB76497.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ANB76497.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 83..228
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 220..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 101302 MW; E6BAB23CFE6D13CB CRC64;
MVNLMCEICG VRRSVARVAL VQNHERRILD VCEFHFERLL RHQRTLSPLE ALFRTDLGGP
VQDDARIVDL STPTAGDSDS MYINEYFSDT VRELLQRAAE RALEFGRSEV DTEHLLYELL
AIPAVAETFN QLHQSATEIQ KLIDETAPKQ SKVVNRRNDR MLVSPRLKSV LQIAYHEARR
QGLGYVGPEH LMIGLAAVPD SFAGNLLRKL GASAQTLRQE LQHQPTGQDK NKKAETSTTP
HLDRFSRDLT SLAREGRIDP VIGRSVEIET MIEILARRRK NNPVLIGEPG VGKTAIVEGL
AIRMVKGDVP DSLRDKRLLE LNINSMVAGS KYRGEFEERV QQLIDEILKN RDALVIFVDE
VHTIVGAGQG GGEGGLDIAN VFKPAMARGE LNLIGATTLA EYQKHIESDS ALERRFQPIL
VSEATVEQSI NILRGLRDRL EGHHHVTIQD DAIVAAATLS DRYVAGRFLP DKAIDLVDQA
AARVHLSATS RPADILEFES EIAQMKREQD YAATRKLFER AHALDSRIKD KEKALSDATD
KWKSKVSCNT SDVSATHIAE IVAKLTGIPV AQLTAAERER LMDLEGRLHH RVIGQGEAVR
AVSDAVRRAR AGLQGSGRPT AVFLFLGPTG VGKTELAKAL AEVVFGDEDA LIRMDMSEYM
ERHAVARLMG APPGYVGYDE GGQLTERVRR RPYSVILFDE IEKAHPDVYN VLLQVFDDGR
LTDGKGRVVD FGNTLMIATS NLGAEIIGGH KRAGLGFMQN DASPSVRGGV MDVLRQHFRP
EFINRVDDII IFESLGQKET LQIVRLQLEQ VKRVASSQDI EITFSEAVVE LLARVGYRPE
FGARELRRQI RQLIENELAR QILDGTLSEG MKVLCELDSE SHKIAFRQQS VPRSESTSDS
SPGNVGPIAV PEG
//
