ID A0A4R7TG48_9ACTN Unreviewed; 875 AA.
AC A0A4R7TG48;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV138_4796 {ECO:0000313|EMBL:TDU91195.1};
OS Kribbella voronezhensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=2512212 {ECO:0000313|EMBL:TDU91195.1, ECO:0000313|Proteomes:UP000295151};
RN [1] {ECO:0000313|EMBL:TDU91195.1, ECO:0000313|Proteomes:UP000295151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2575 {ECO:0000313|EMBL:TDU91195.1,
RC ECO:0000313|Proteomes:UP000295151};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-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}.
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:TDU91195.1}.
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DR EMBL; SOCE01000001; TDU91195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R7TG48; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295151; 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:TDU91195.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDU91195.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295151};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 87..114
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 410..504
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 875 AA; 97717 MW; 478FFE419C0C41CD CRC64;
MDMNRLTQKS QEALHDAQTK ALRFGHSQID GEHLLLALLD QPDGLAPRLL AQAGADPDGL
RDRLEQELSR RPKVSGPGAE PGQVLVTQRL SRLLDAADRE AKRLKDEYVS IEHLVIALLD
EGRQSTSGRL LAEQGLTRDG FLSALTTVRG NQRVTSAMPE ASYEALDKYG RDLVKDAAEG
RLDPVIGRDN EIRRVVQILS RKTKNNPVLI GDPGVGKTAI VEGLAQRIAN GDVPEGLRNR
TVFALDMASL VAGAKYRGEF EERFKAVLNE VKAAEGRVLL FVDELHTVVG AGATEGAMDA
GNMLKPMLAR GELHMIGATT LDEYRMHVEK DAALERRFQP VVVDEPTVED AISILRGLRE
RLEVFHGVKI QDAAMVAAVV LSHRYISDRF LPDKAIDLVD EACAMLRTEI DSMPAELDEL
TRRVRRLEIE EAALAKEEDA ASRQRLDELR KELADLRSEA DAMHAQWDAE RQALRKVQTL
RQQMEQVRQE AEQAERDYDL NRAAELRHGR LPDLERQLAA EEERLATKQH GHRLLREVVT
EEEIASIVSR WTGIPVSRLQ EGEREKLLRL DEVLHERLVG QDEAVQLVAD AIVRARSGIK
DPRRPIGSFI FLGPTGVGKT ELAKTLAAAL FDTEENIVRI DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HPDVFNTLLQ ILDDGRLTDA QGRTVDLRNT
VIIMTSNIGS AYLLDGVTAD GQVKEDARDA VMDELRRQFR PEFLNRVDEI VLFKPLTMAE
IERIVDLMFD DLRTRLADRR MTLEVEPEAA RHIAAQGFDP VYGARPLRRF IAREVETRIG
RALLGGDILD GAVIRVTVHD GEIAVSHENP VEVAA
//