ID A0A1V4IHL2_9CLOT Unreviewed; 869 AA.
AC A0A1V4IHL2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:OPJ59007.1};
GN ORFNames=CLORY_34970 {ECO:0000313|EMBL:OPJ59007.1};
OS Clostridium oryzae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ59007.1, ECO:0000313|Proteomes:UP000190080};
RN [1] {ECO:0000313|EMBL:OPJ59007.1, ECO:0000313|Proteomes:UP000190080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ59007.1,
RC ECO:0000313|Proteomes:UP000190080};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium oryzae DSM 28571.";
RL Submitted (MAR-2017) 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:OPJ59007.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MZGV01000052; OPJ59007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4IHL2; -.
DR STRING; 1450648.CLORY_34970; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000190080; 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:UP000190080};
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 417..504
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 97862 MW; 19C1B7E09E92513E CRC64;
MNIDKMTVKV QQALSDAQAA AVKFNHQQVD VIHLFYALIS DDEGLIPNVL GKMSTNVEAM
RNSTKKVLDG MPKVLGDAAG ASSVYATRKI EEVLVKASDI ANDFKDMYIS VEHLMISIMD
VDKKGSTGQI LAQYGVNKTA FLETLKSIRG NQRVESQDPE GTYEALVKFG RNLVEDAKKH
KLDPVIGRDD EIRRAIRILS RRTKNNPILI GEPGVGKTAI VEGLAERIVR GDVPEGLKNK
IIFSLDMGSL IAGAKFRGEF EERLKAVLKE VEKSEGKIIL FIDEIHTIVG AGKGDGAMDA
GNIIKPMLAR GELHCIGATT FDEYRKYIEK DKALERRFQP VTVEQPTVED TISILRGLKE
RFEIHHGIRI HDSAIVSAAK LSDRYITDRF LPDKAIDLID EAGAMIRSDI DSMPSELDAV
KRKVFQLEIE KETLSKENDF ASQERLRNLE KELSNLKEKD AEMTAKYEKE KSFIKDIREL
KEKLDEARGD LEQYERNYEL NKVAEYKYGV IPKLESDIEE KEKQLKENYE GALLKEEVTE
EEIADIVSKW TGIPVTKLQE GEKVKLLKLE DQLSKRVIGQ EEAVKSVTNC VIRARAGIKD
NKKPIGSFIF LGPTGVGKTE LAKTLANTLF DSEKNIIRID MSEYMEKYSV SRLIGAPPGY
VGYEEGGQLT EAVRRSPYSV ILFDEIEKAH DDVFNIFLQV LDDGRLTDNK GNLIDFKNTI
IIMTSNIGSD YLLENTEKDS IDDEIREQVM DELKDRFKPE FLNRLDDIIL FKPLGADAIK
KIIDLFINEF AVRLSERNIS ITVTDAAKEI MISEGYDPIY GARPMRRYIE NTLETDIAKK
IIAGEVYDGC HMVIGSNNGQ IEIKVSNDK
//
