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Database: UniProt
Entry: A0A1E8FS52_9MICC
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ID   A0A1E8FS52_9MICC        Unreviewed;       889 AA.
AC   A0A1E8FS52;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=BIU82_17715 {ECO:0000313|EMBL:OFI38782.1};
OS   Arthrobacter sp. SW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1920889 {ECO:0000313|EMBL:OFI38782.1, ECO:0000313|Proteomes:UP000176251};
RN   [1] {ECO:0000313|EMBL:OFI38782.1, ECO:0000313|Proteomes:UP000176251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW1 {ECO:0000313|EMBL:OFI38782.1,
RC   ECO:0000313|Proteomes:UP000176251};
RA   Shaligram S.M., Kumbhare S.V., Pawar S., Dhotre D., Muddeshwar M.G.,
RA   Kapley A.;
RT   "Genomic insights of Arthrobacter sp. strain SW1 for secondary metabolite
RT   production.";
RL   Submitted (SEP-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}.
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:OFI38782.1}.
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DR   EMBL; MJLT01000010; OFI38782.1; -; Genomic_DNA.
DR   RefSeq; WP_070348779.1; NZ_MJLT01000010.1.
DR   AlphaFoldDB; A0A1E8FS52; -.
DR   STRING; 1920889.BIU82_17715; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000176251; 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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176251};
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   REGION          866..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          399..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   889 AA;  95456 MW;  A638665EF827C653 CRC64;
     MDVKFTTKSQ EALSAAAMNA STAGNPQLEP AHLLKALMDQ REGVAVALLR ATGADPDAVS
     VQASSAIKAL PSSSGSSVQQ AQLSRPALQA IKAAESEAEK LGDSFVSTEH LLLGLSAGSD
     AVGKLLRDAG ASHEALLAAL PGVRGDRKVT SPDPENTFQA LEKFGTDLTA VARSGKLDPV
     IGRDSEIRRV IQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRMVAGDVPE SLRGKTLIAL
     DLASMVAGAK YRGEFEERLK AVLEEIKNSD GQIVTFIDEI HTVVGAGASG ESAMDAGNML
     KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVYVG EPSVDDTIGI LRGLKERYEA
     HHKVAIADSA LVAAATLSNR YIAGRQLPDK AIDLVDEAAS RLRMEIDSAP EEIDQLRRAV
     DRLTMEELAL AGESDAASVE RLAALRADMA DKKETLAALN ARWEAEKAGL NRVGDLKAKI
     DELRSAAEKY QREGDLESAS RILYGELPAL ERELNAAAAE EAAQDKPELM VAEEVTADDI
     AEVISAWTGI PAGRMLQGES QKLLHMEEEL GKRLIGQHKA VTAVSDAVRR ARAGISDPNR
     PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMIRIDMSE YGEKHSVARL VGAPPGYVGY
     EEGGQLTEAV RRRPYSVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNTILVL
     TSNSGSQFLV DPSLDARAKQ DAVMSVVRAS FKPEFLNRLD EIVLFDPLSV DELANIVELH
     VAELAKRLHD RRLTLEVSDG ARAWLAMTGY DPAYGARPLR RLVQREIGDR LAKEILAGEI
     VDGDTVLVDT AADVDELTIE GLEALEGPDG GAPAGSGLAG SGLVVRRKQ
//
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