ID A0A0B2ALM1_9MICC Unreviewed; 879 AA.
AC A0A0B2ALM1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=LK10_06880 {ECO:0000313|EMBL:KHL04251.1};
OS Sinomonas humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL04251.1, ECO:0000313|Proteomes:UP000030982};
RN [1] {ECO:0000313|EMBL:KHL04251.1, ECO:0000313|Proteomes:UP000030982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL04251.1,
RC ECO:0000313|Proteomes:UP000030982};
RA Lee L.-H.;
RT "Genome sequence of Sinomonas sp. MUSC 117.";
RL Submitted (SEP-2014) 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:KHL04251.1}.
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DR EMBL; JTDL01000082; KHL04251.1; -; Genomic_DNA.
DR RefSeq; WP_043121406.1; NZ_JTDL01000082.1.
DR AlphaFoldDB; A0A0B2ALM1; -.
DR STRING; 1338436.LK10_06880; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000030982; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000030982};
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 399..500
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 879 AA; 94889 MW; 618BC935DF1A2B69 CRC64;
MDVKFTTKSQ EALSAAAMNA STAGNPQVEP AHLLKALMDQ RDGVAVALLR ATGADPDAVS
VAASTAIKAM PSTSGSTVAQ AQLSRQGLQV IHVAQQESEQ MGDSFVSTEH LLLGLAADGG
AAGKALRDAG ATLESLKAAL PGVRGDRKVD SPDPENTFQA LEKYGTDLTA IARSGKLDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRGKTLIAL
DLGSMVAGAK YRGEFEERLK AVLEEIRSSE GQIVTFIDEI HTVVGAGATG DSSMDAGNML
KPMLARGELR LIGATTLDEY RENIEKDAAL ERRFQQVFVG EPSVEDTIAI LRGLKERYEA
HHKVAIADSA LVAAASLSNR YISGRQLPDK AIDLVDEAAS RLRMEIDSAP EEIDQLRRAV
DRLTMEELAL DGETDEGSIE RLAAIREDMA NKKEELAALN SRWEAEKAGL NRVGELKAKL
DELRSLADKA QREGDLAEAS RILYGEIPTL DRELKEASAV EEQVSGKAKM VAEEVTADDI
AEVISAWTGI PAGRMLQGES QKLLHMEEEL GKRLIGQKKA VEAVSDAVRR ARAGISDPNR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YSEKHAVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVILL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNTILVL
TSNLGSQFLV DPDLSEATKR DAVMGVVHSS FKPEFLNRLD DVIMFDPLSV DELARIVQLQ
VDSLQQRLHE RRLTLDVTDG ARAWLAMTGY DAAYGARPLR RLVQREIGDR LAKELLSGEI
ADGDTVLVDV ADVSVDLQDL TGATSGLSVT RKAPASQEA
//
