ID A0A0Q8YDI3_9MICO Unreviewed; 853 AA.
AC A0A0Q8YDI3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ASE25_03070 {ECO:0000313|EMBL:KRC92348.1};
OS Terrabacter sp. Root85.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Terrabacter.
OX NCBI_TaxID=1736603 {ECO:0000313|EMBL:KRC92348.1, ECO:0000313|Proteomes:UP000051752};
RN [1] {ECO:0000313|Proteomes:UP000051752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root85 {ECO:0000313|Proteomes:UP000051752};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC92348.1, ECO:0000313|Proteomes:UP000051752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root85 {ECO:0000313|EMBL:KRC92348.1,
RC ECO:0000313|Proteomes:UP000051752};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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|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:KRC92348.1}.
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DR EMBL; LMIW01000001; KRC92348.1; -; Genomic_DNA.
DR RefSeq; WP_056772136.1; NZ_LMIW01000001.1.
DR AlphaFoldDB; A0A0Q8YDI3; -.
DR STRING; 1736603.ASE25_03070; -.
DR Proteomes; UP000051752; 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 104; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..155
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 404..484
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 853 AA; 92465 MW; B36769E8F21A9D1B CRC64;
MDLQLTNKAQ EAFAQAATTA TGKHHPNIEP AHLLLALAAQ SGTTTPALLT AGGSSVAAAT
AVAERAMAAM PQVTGGAQQP QLSATAGRVV QQAQQYMTAM GDSYVSTDHL LLALARTGQF
GLDADAIEGA IPELRGGRPV TSDNPEGTFE ALSKYGTDLT ARAREGKLDP VIGRDAEIRR
VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVEGDVP ESLRDKTLYS LDLGSMIAGA
KYRGEFEERL KAVLEEIKGS DGQIVTFIDE IHTVVGAGAG GEGAMDAGNM LKPMLARGEL
RLVGATTLDE YRKHIEKDAA LERRFQQVFV GEPSVEDTIA ILRGLKERYE GHHKVTIADS
ALVAAASLSD RYISGRQLPD KAIDLIDEAA SRLRMEIDSS PVEIDELRRA VDRLKMEEFA
LEQESDAASK DRLERLRKDL ADRSEELAAL NARWEAEKSG LNAVGDLKAR VDDLRTQADR
LQREGDLGAA SKILYGDIPT LEKELATAQE REAAATTGDE EPMVKEEVGA DDIADVISAW
TGIPAGRLME GESEKLLHME QHIGARLIGQ ADAVRAVSDA VRRTRAGVSD PDRPTGSFLF
LGPTGVGKTE LAKSLADFLF DDERAMVRID MSEYSERHSV ARLIGAPPGY VGYEEGGQLT
EAVRRRPYSV ILLDEVEKAH PETFDILLQV LDDGRLTDGQ GRTVDFRNVI LVLTSNLGSQ
FLTDPTLSPD ARRESVMGVV RSSFKPEFLN RLDEVVVFDA LSRDDLAHIV DLQVRAFAER
LSDRRITLEV TDDARQWLAA RGYDPAYGAR PLRRLVQREI GDRLARGLLS GEVRDGSTVA
VGVDPDGEAL DLV
//