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Database: UniProt
Entry: A0A4R7TG48_9ACTN
LinkDB: A0A4R7TG48_9ACTN
Original site: A0A4R7TG48_9ACTN 
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
//
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