ID A0A3L8NY29_9ACTN Unreviewed; 861 AA.
AC A0A3L8NY29;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RLV47834.1};
GN ORFNames=D9V37_17070 {ECO:0000313|EMBL:RLV47834.1};
OS Nocardioides mangrovicus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2478913 {ECO:0000313|EMBL:RLV47834.1, ECO:0000313|Proteomes:UP000281708};
RN [1] {ECO:0000313|EMBL:RLV47834.1, ECO:0000313|Proteomes:UP000281708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4Q3S-7 {ECO:0000313|EMBL:RLV47834.1,
RC ECO:0000313|Proteomes:UP000281708};
RA Li F.;
RT "Marmoricola sp. 4Q3S-7 whole genome shotgun sequence.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV47834.1}.
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DR EMBL; RDBE01000010; RLV47834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8NY29; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000281708; 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:UP000281708};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 93747 MW; 62B271AEAA231064 CRC64;
MDANKFTKRS VEAINDAQTM AVTAGNAQTE PIHLLAALLR QEQGVAGALL TKAGTDPTSI
ARAADDAVAR LPKASGSAVQ TPAASGALTR VLAKAISVAE AMKDDYAATE HLLLGLDNVD
SSAKQLLDDA GLTEQALREA VVATRGDRRV TSQDAEATYE ALEKYAVDLT ARAEEGSLDP
VIGRDAEIRR VIQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVDNDVP DSLKGRRLLS
LDLAAMVAGA KYRGEFEERL KAVLDEIKAS AGQVITFIDE LHTVVGAGAG GEGAMDAGNM
LKPMLARGEL RLIGATTLDE YREHIEKDPA LERRFQQVYV GEPSVEDTVA ILRGLQEKYE
AHHGVTITDA ALVAAAMLSD RYITGRQLPD KAIDLVDEAA SRLRMEIESS PVEIDELRRQ
VDRMRMEELA LERETDDASV DRLERLRADL ADREEILRGL EARWEAERAT LEGAGDLRKQ
RDTLRTQAER MQREGDLAGA SEILYGRIPE IEKQIEAAEA SEAVETERLV NENVGPQEIA
DVVESWTGIP TGRLLEGETA KLLRMEDIIG ERLIGQRAAV AAVSDAVRRS RAGISDPDRP
AGSFLFLGPT GVGKTELAKS LADFLFDDER AIVRIDMSEY SEKHSVSRLV GAPPGYIGYN
EGGQLTEAVR RRPYSVVLLD EVEKAHPEVF DILLQVLDDG RLTDGQGRTV DFRNTLLILT
SNLGSSFLVD PTLDDDKKRE SVLAVVRQAF KPEFLNRLDE IVMFDALSQD DLAHIVDLQL
HAFDARLAPR RITVTVTDAA RAWLTSTGYD PLYGARPLRR LVQTAIGDPL ARMLIGGEVA
DGQQVSVDRV EEGDGLVLLV G
//
