ID A0A239G5E0_9ACTN Unreviewed; 865 AA.
AC A0A239G5E0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN06265355_12326 {ECO:0000313|EMBL:SNS64321.1};
OS Actinomadura mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS64321.1, ECO:0000313|Proteomes:UP000198420};
RN [1] {ECO:0000313|EMBL:SNS64321.1, ECO:0000313|Proteomes:UP000198420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS64321.1,
RC ECO:0000313|Proteomes:UP000198420};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNP01000023; SNS64321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239G5E0; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000198420; 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:SNS64321.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNS64321.1};
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 84..111
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 412..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 95250 MW; 7E13FBBCC5E1283C CRC64;
MDYKLTQKSQ EALSVAVRRA AAEGHPEVEP QHLLVALIGL PDGTAVPLLE AVGADWQVVR
RRAEEQLAAM PKAQGSTVAT PRLSGQLQRS VNTAANRAQQ LEDEYVSTEH LLVGLAADGG
PAAGLLKEFG AAPEALLEAF EKVRGHARVT SENPEGTYQS LEKYGVDLTA AARDGRLDPV
IGRDPEIRRV IQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIIAGDVPE SLRGKRLVSL
DLGAMVAGAK YRGEFEERLK AVLNEIKKSE GQVVTFIDEL HTVVGAGAAE GAMDAGNMLK
PMLARGELRM IGATTLDEYR ERIEKDAALE RRFQQVFVGE PTVEDTIAIL RGLKGRYEAH
HKVQINDSAM VAAATLSDRY ITSRFLPDKA IDLVDEAASR LRMEIDSRPV EVDELQRAVD
RLKMEQMNLE KETDEASRQR LERLRADLAD RQEQLSGVNA RWEREKAELN RVGEIKERID
QLRGEAARAE RDGDLETSSR LVYGEIPALE KQLEEAAEAT ETRDTMVKEE VGPDDVADVV
ASWTGIPAGR LLEGETAKLL RMEDDLGRRL IGQEAAVRTV SDAVRRARAG ISDPDRPTGS
FLFLGPTGVG KTELAKALAE FLFDDERAMT RIDMSEYSEK HSVARLVGAP PGYIGYEEGG
QLTEAVRRRP YSAVLLDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR NTILILTSNI
GSQFLVDPTL ENGAKREAVW NAVRNSFKPE FLNRLDDVIL FDALSTEELT RIVDLQVDRL
ADRLADRQLA LRVTPAAREW LALTGYDPLY GARPLRRLVQ TAIGDQLARE LLSGEVRDGD
EVVVDLDEAA DRLTVERSGG LNLTK
//