ID A0A031IDK3_9BACL Unreviewed; 858 AA.
AC A0A031IDK3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BW42_02813 {ECO:0000313|EMBL:EZP58510.1};
OS Exiguobacterium sp. RIT341.
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1470592 {ECO:0000313|EMBL:EZP58510.1, ECO:0000313|Proteomes:UP000023864};
RN [1] {ECO:0000313|EMBL:EZP58510.1, ECO:0000313|Proteomes:UP000023864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT341 {ECO:0000313|EMBL:EZP58510.1,
RC ECO:0000313|Proteomes:UP000023864};
RA Gan H.Y., Gan H.M., Savka M.A., Hudson A.O.;
RT "Draft Genome Sequences of 13 Willow Endophytes.";
RL Submitted (MAR-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|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU362034}.
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:EZP58510.1}.
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DR EMBL; JFYW01000011; EZP58510.1; -; Genomic_DNA.
DR RefSeq; WP_035412327.1; NZ_JFYW01000011.1.
DR AlphaFoldDB; A0A031IDK3; -.
DR PATRIC; fig|1470592.3.peg.2724; -.
DR Proteomes; UP000023864; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Hydrolase {ECO:0000313|EMBL:EZP58510.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362034}; Protease {ECO:0000313|EMBL:EZP58510.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..491
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 96110 MW; 3190ADF7DE1D807E CRC64;
MDFERLTNRA HEGIVSAQAI AKQRRHSEIT EWHLLLALLA QEEGIARVIF EKLNQRIETL
NAAIDEAIGK LPALSQATTP RIGGSLLNVL TEAETEARLM QDDYVSVEHL LLALIKQSSP
ATQYLRRQGI TEETLREAIV SMRGNRKVTT KNPEETFDVL KKYGRDLVAD FRSGKTDPVI
GRDDEIRRVI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVRGDVPES LKNKQLFSLD
MSALVAGAKY RGEFEERLQA VLNEVKEAEG QILLFIDELH TIVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLDEYRK YIEKDPALER RFQQVLVAEP DVEDTISILR GLKERFEIHH
GVRIHDNALV AAAMLSDRYI TDRFMPDKAI DLVDEACAMI RTDMESMPAE LDSLVRRVMQ
LEIEEAALKK ETDEASRKRL AVLQQELSSA REDESALRTR WEREKESSQS VQQLRADLEK
AKLALQEAEG RYDLNRASEI KYGQIPDLEA RLKVAEESSE HVSHELVREA VTEEEISDIV
SKWTGIPVTR LAQGEREKLL YLEDTLHERV FGQDEAVRLV ADAVIRARAG IKDPNRPIGS
FLFLGPTGVG KTELAKALAA AMFDSEDHIV RIDMSEYMEK HNVSRLVGAP PGYVGYEEGG
QLTEAVRRSP YSVLLFDEIE KAHGDVFNIL LQLLDDGRLT DAQGRVVDFK NTIVIMTSNI
GAPILLEAAK DGVIDAAEEE AVRQELKRHF RPEFLNRIDD TILFHPLHRT EIERIIDKAV
EKMTSRLSGR GITINVTDAA KTLIFEEAFE PQYGARPINR YMQRTIETKL ARALISGAIQ
DGSQIAIDVA DGELVVNG
//
