ID A0A1R4G4K6_9MICC Unreviewed; 870 AA.
AC A0A1R4G4K6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FM101_07565 {ECO:0000313|EMBL:SJM62932.1};
OS Arthrobacter rhombi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=71253 {ECO:0000313|EMBL:SJM62932.1, ECO:0000313|Proteomes:UP000195913};
RN [1] {ECO:0000313|EMBL:SJM62932.1, ECO:0000313|Proteomes:UP000195913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B Ar 00.02 {ECO:0000313|EMBL:SJM62932.1,
RC ECO:0000313|Proteomes:UP000195913};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FUHW01000027; SJM62932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4G4K6; -.
DR Proteomes; UP000195913; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000195913};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 438..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 94387 MW; 7C0F111366FEBAE9 CRC64;
MDAKFTTKSQ EALSAAGMNA STAGNAQVEP AHLLKALMDD RGSLAVELLK KAGVDPDSVS
VAASGAIRDL PASSGSTVAQ AQYSRSFLQV INAATTAASD LGFSRVSAEH LLLGLAADAG
KTGEILRSAG ASEQSLKAAV EGLRGDHPRD TEDPESTFEA LEKFGTDLTA IARSGKLDPV
IGRDAEIRRL VQVLSRRTKN NPVLIGDPGV GKTAVVEGLA QRMIAGDVPE SLRGKTLIAL
DLGSMVAGAK YRGEFEERLK AVLEEIRDSD GQIVTFIDEI HTVVGAGASE GAMDAGNMLK
PMLARGELRL IGATTLDEYR QNIEKDPALE RRFAQVYVGE PSVDDTIGIL RGLKERYEAH
HKVEIADSAL VAAATLSNRY ISGRQLPDKA IDLVDEAASR LRMEIDSAPE EIDELRRVVD
RMTMEELALK GESDPASRER LEALRADMAD RRERLDALNA RWEAEKAGLN RVGDLKVQLD
ELRSRAERIQ REGDLEKASR LLYGEIPELQ RQLDAAQAEE AEGAHEETMV SDEVTADDIA
DVISAWTGIP AGRMLQGESQ KLLDMESLLG QRLIGQGSAV TAVSDAVRRS RAGIADPDRP
TGSFLFLGPT GVGKTELAKA LADFLFDDEH AMVRIDMSEY SEKHSVSRLV GAPPGYVGYE
EGGQLTEAVR RRPYSVILLD EVEKAHPEVF DILLQVLDDG RLTDGQGRTV DFRNTILVLT
SNLGSQFLVD PHLADDAKRE AVMNIVNTSF KPEFLNRLDD VILFDPLSLE QLGRIVEIQV
ATLSRRLAER RLTLRVNDEA RQWLAKTGYD PAYGARPLRR LVQREIGDRL AKSVLSGEIV
DGDTVDVQLD ADQGALTIHR SAGPEGPTAS
//
