ID A0A1M6N555_9ACTN Unreviewed; 870 AA.
AC A0A1M6N555;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421803_11166 {ECO:0000313|EMBL:SHJ90831.1};
OS Nocardiopsis flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=758803 {ECO:0000313|EMBL:SHJ90831.1, ECO:0000313|Proteomes:UP000184452};
RN [1] {ECO:0000313|EMBL:SHJ90831.1, ECO:0000313|Proteomes:UP000184452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHJ90831.1,
RC ECO:0000313|Proteomes:UP000184452};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|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; FQZK01000011; SHJ90831.1; -; Genomic_DNA.
DR RefSeq; WP_073380575.1; NZ_FQZK01000011.1.
DR AlphaFoldDB; A0A1M6N555; -.
DR STRING; 758803.SAMN05421803_11166; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000184452; 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 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 Hydrolase {ECO:0000313|EMBL:SHJ90831.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHJ90831.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184452};
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 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 95536 MW; 3AAAE1B06C020066 CRC64;
MNYKLTQKSQ EALSVAIRRA TTDGNPQTEP VHLLAALLDQ AEGITRPLLK EVGADPDRLK
DRVDAAIGAL PKVSGSTTAS PSSSRQLIVS INTAAQRAKQ MEDEYVSTEH LLVGLAADGG
EAARLLKDAG AAPEALLDAF ERVRGKGRIT TENPEETYQA LEKYGVDLTE RAREGKVDPV
IGRDGEIRRV IQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPQ SLLGKKLISL
DLSAMVAGAK YRGEFEERLK AVLQEIKDSD GQVITFIDEL HTMVGAGASG DGSMDAGNML
KPMLARGELR MVGATTLDEY RERIEKDPAL ERRFQQVFVG EPSATDTIAI LRGLKGRYEA
HHKVQISDSA LVAAATLSDR YITARFLPDK AIDLIDEAAS RLRMEIDSSP VEIDELRRTV
DRLKMEEMAL DKESDTASRQ RLERLRSDLA DRQERLNGLV ARWEQEKAGL NRVGELKGRL
DELRTRAELA EREGDFTTAS RLMYGEIPQL EKQLEEAAQA EESTGPETDT MVKDEVGADE
VAEVVSSWTG IPVGRMMEGE TSKLLRMEDE LGRRLIGQRD AVVAVADAVR RARAGISDPD
RPTGSFLFLG PTGVGKTELA KALADFLFDD ERAIVRIDMS EYSEKHSVSR LVGAPPGYVG
YEEGGQLTEA VRRRPYTVVL LDEVEKAHIE VFDTLLQVLD DGRLTDGQGR VVDFRNTILI
LTSNLGSQFL VDQTLDEATR GQRVMDVVRA TFKPEFLNRL DDVIMFDALS IEDLTRIVDL
QVDRLARRLA DRRLHLDVTP GAREWLAMTG YDPNYGARPL RRLVQSSIGD PLARELLSGR
LAEGDTVVVD VNDAADSLVV TARPIGSPAG
//