ID A0A1H1EH66_9MICC Unreviewed; 867 AA.
AC A0A1H1EH66;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04489742_2935 {ECO:0000313|EMBL:SDQ88092.1};
OS Arthrobacter crystallopoietes.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=37928 {ECO:0000313|EMBL:SDQ88092.1, ECO:0000313|Proteomes:UP000181917};
RN [1] {ECO:0000313|EMBL:SDQ88092.1, ECO:0000313|Proteomes:UP000181917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20117 {ECO:0000313|EMBL:SDQ88092.1,
RC ECO:0000313|Proteomes:UP000181917};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNKH01000002; SDQ88092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1EH66; -.
DR STRING; 37928.SAMN04489742_2935; -.
DR Proteomes; UP000181917; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SDQ88092.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDQ88092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000181917};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 2..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 399..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 93565 MW; 524E52811AA0C144 CRC64;
MLDAKFTTKS QEALSSAAMN ASTVGNPQVE PAHLLKALMD QREGVAVALL KAAGSDPDAV
SVQASSAIKA LPASSGTSVA QAQYSRGILQ VINVAKQEAE RLGDSYISTE HLLLGLAADS
AATGKILQNA GASHEALRAA LSGVRGDRKV DSADPENTFQ ALEKFGVDLT AIARSGKLDP
VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP ESLRGKTLIS
LDLGSMVAGA KYRGEFEERL KAVLEEIKNS DGQIVTFIDE LHTVVGAGAS EGSMDAGNML
KPMLARGELR MIGATTLDEY RENVEKDPAL ERRFQQVYVG EPSVDDTIGI LRGLKERYEA
HHKVSIADSA LVAAATLSNR YIAGRQLPDK AIDLVDEAAS RLRMEIDSAP EEIDQLRRAV
DRLTMEELAL ADETDVASQE RLEALRADMA DKKEQLAALN ARWEAEKAGL NRVGDLKAKL
DELRSLADKA QRDGDLAEAS RILYGEIPAL QKDLDAAQAA ETETEAPELM VSEEVGADDI
AEVISAWTGI PAGRMLQGES QKLLQMEQFI GGRLIGQTKA VASVSDAVRR ARAGISDPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YSEKHSVSRL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNVILVL
TSNMGSQFLV DPMLDDGQKR EAVMKVVNAS FKPEFLNRLD DVIMFDPLSI EELSRIVDLQ
VQSLAARLNE RRLTLEVTDG AREWLALTGF DPAYGARPLR RLVQREIGDR LARGLLSGDI
SDGDTVLVDV AEASLEGGAE GLTVRAK
//
