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
//