ID A0A516Q4T4_9ACTN Unreviewed; 871 AA.
AC A0A516Q4T4;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QDP98449.1};
GN ORFNames=FOE78_23370 {ECO:0000313|EMBL:QDP98449.1};
OS Microlunatus elymi.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=2596828 {ECO:0000313|EMBL:QDP98449.1, ECO:0000313|Proteomes:UP000319263};
RN [1] {ECO:0000313|EMBL:QDP98449.1, ECO:0000313|Proteomes:UP000319263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUDC0627 {ECO:0000313|EMBL:QDP98449.1,
RC ECO:0000313|Proteomes:UP000319263};
RA Ghim S.-Y., Hwang Y.-J., Son J.-S., Shin J.-H.;
RT "Microlunatus dokdonensis sp. nov. isolated from the rhizospheric soil of
RT the wild plant Elymus tsukushiensis.";
RL Submitted (JUL-2019) 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}.
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DR EMBL; CP041692; QDP98449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A516Q4T4; -.
DR KEGG; mik:FOE78_23370; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000319263; Chromosome.
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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000319263};
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 REGION 516..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 95061 MW; 33DB8ED3E37CE3AB CRC64;
MEAEKLTTKS RDAVSAALRS ALLAGNPNAE PEHLLSALLS VPQNTVGPLL SAVGADPAKI
NASAQEAIAK LPSAKGNSVS QPGLSGSMAR VLADAESRAE QLGDSFVATE HLLISLAAVD
SEAKRILSAD GVDADKLVAA FNESRGSKRV TSAEAEGTSS ALDQYGVDLT EQAREGKLDP
VIGRDTEIRR VVQVLARRTK NNPVLIGEPG VGKTAVVEGL AHRLVAGDVP DSLKGRRLIS
LDLASMVAGA KYRGEFEERL KAVLTEIRDA EGQVITFIDE LHTVVGAGAT GEGAMDAGNM
LKPMLARGEL RMIGATTLDE YRERIEKDPA LERRFQQVFV GEPSVEDTIA ILRGLRERYE
AHHKVAITDG ALVAAASLSN RYITSRQLPD KAIDLIDEAA SRLRMEIDSS PEEIDQLRRQ
VERMRMQEFA LAKETDPGSA ERLHRLREDL ANSEEQLRGL EQRWEAEKEG LNQVGDLKKQ
IDELRGEAER AQREGDLGRA SELLYGRIPA LQKQLEKADE EEKVAEESGN GPMVSEEVGP
NDVAEVVSNW TGIPVGRLLQ GESEKLLSME DRLGERLIGQ KQAVRAVSDA VRRSRAGISD
PNRPTGSFLF LGPTGVGKTE LAKSLAEFLF DDEHAMIRID MSEYSEKHSV ARLVGAPPGY
VGYEEGGQLT EAVRRRPYAV VLLDEVEKAH PEIFDILLQV LDDGRLTDGQ GRTVDFRNVI
MILTSNLGSQ FLADQTMDAE AKETAVMNVV RASFKPEFLN RLDEVVLFDA LGTEELSKIV
DININRLNER LADRRIKVDV TDGARDWLAL TGFDPTYGAR PLRRLIQTTI EDQLAREVLA
GRIAEGDTVT FDVEDQSDGL VIVPSRQVAT I
//