ID A0A543CL35_9ACTN Unreviewed; 865 AA.
AC A0A543CL35;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FB559_3420 {ECO:0000313|EMBL:TQL97814.1};
OS Actinoallomurus bryophytorum.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinoallomurus.
OX NCBI_TaxID=1490222 {ECO:0000313|EMBL:TQL97814.1, ECO:0000313|Proteomes:UP000316096};
RN [1] {ECO:0000313|EMBL:TQL97814.1, ECO:0000313|Proteomes:UP000316096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 102200 {ECO:0000313|EMBL:TQL97814.1,
RC ECO:0000313|Proteomes:UP000316096};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-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|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:TQL97814.1}.
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DR EMBL; VFOZ01000001; TQL97814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A543CL35; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000316096; 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 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 Hydrolase {ECO:0000313|EMBL:TQL97814.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TQL97814.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000316096};
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 412..533
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 94875 MW; 23DE0289BDF9D02F CRC64;
MDYKLTQKSQ EAVSTAVRRA ATEGHPQVEP AHLLVALLSQ GDGTARPLLE AVGADPQALR
RRAEEQIDAL PKAAGSTVGA PQTSRPLLVV LNTAANRAKQ LEDEYVSTEH LLVGLASDGG
PVATLLRENG ATPDALLEAF EQVRGHARVT SENPEETYQA LEKYGVDLTA QAREGKLDPV
IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE TLKNKQLISL
DLSAMVAGAK FRGEFEERLK AVLNEIKQSD GRVVTFIDEL HTMVGAGAAE GSMDAGNMLK
PMLARGELHM IGATTLDEYR ERIEKDSALE RRFQQVLVGE PSVEDTIAIL RGLKGRYEGH
HEVQIADAAL VAAAALSDRY ITARFLPDKA IDLVDEAASR LRMEIDSRPV EIDELQRVVD
RLEMEQHQLS KESDEASQQR HERLKAELAD RREQLNGLNA RWAQEKEGLN KVGELKKRID
EAESRREQAF RQAQVDGDWK APSDIAIEIK QLRDDLEAAA EAAKNRDAMV REEVTADDVA
EVVAAWTGIP AGRLLEGETA KLLRMEEELG RRLIGQSDAV RAVSDAVRRA RAGVSDPDRP
TGSFLFLGPT GVGKTELAKA LADFLFDDER ATVRIDMSEY GEKHSVARLV GAPPGYVGYE
EGGQLTEAVR RRPYCVVLLD EVEKAHPEVF DVLLQVLDDG RLTDGQGRTV DFRNTILIMT
SNLGSQFLVD PALDNGARRE AVLTAVRGNF KPEFLNRLDD VIIFDALTTE ELTKIVDLQV
DRLARRLSDR RLTLTVTDGA REWLALTGFD PAYGARPLRR LVQSAIGDQL ARELLSGEIR
DGDEVVVDVD EAADTLTVKP GVPVA
//
