ID A0A1Y0CYQ3_9GAMM Unreviewed; 859 AA.
AC A0A1Y0CYQ3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=CBP12_07685 {ECO:0000313|EMBL:ART80037.1};
OS Oceanisphaera avium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanisphaera.
OX NCBI_TaxID=1903694 {ECO:0000313|EMBL:ART80037.1, ECO:0000313|Proteomes:UP000243793};
RN [1] {ECO:0000313|Proteomes:UP000243793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMac2203 {ECO:0000313|Proteomes:UP000243793};
RA Sung H.;
RL Submitted (MAY-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}.
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DR EMBL; CP021376; ART80037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0CYQ3; -.
DR KEGG; ocm:CBP12_07685; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000243793; Chromosome.
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:UP000243793};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 95791 MW; 935A56624A4DC1E8 CRC64;
MRLDRLTSKF QLALQDAQSM AVGRDHAYIE PAHLLIAMLN QEGGSLRPLL TNAGVDGNTL
RVELDKSVER LPKVSGANMD VQVSPVLARL LNQCDKLAQQ RKDSYISSEL FLLAALDEQG
ELGELLKRAG LSKEKLNKAI DEVRGGQKVD DPNAEENRQA LEKYTIDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGAPGV GKTAIAEGLA QRIINGEVPE GLKGKRVLSL
DMGALIAGAK YRGEFEERLK ALLNELAKEE GQVILFIDEL HTMVGAGKGE GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLINE PSVEDTIAIL RGLKERYELH
HHVQITDPAI VAAAVLSHRY IADRQLPDKA IDLIDEAASS IRLQIDSKPE PLDKLDRRII
QLKLEEQALL KEDDEGSIKR LQLIRDELSD KEGEYADLEE IWLSEKAAMA GTQHIKSELE
QVRRELEVAR RAGDLGRMSE LQYGRIPELE KQLDLAGQAE MQEQHLLKNR VTDEEIADVL
SRWTGIPVAK MLEGEKDKLL RMEDSLHQQV IGQDEAVDAV SNAIRRSRAG LSDPNRPVGS
FLFMGPTGVG KTELCKALAD FLFDSRDAMI RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNI
GSDLIQEHNH DTAYDEMKEL LMGVLSQQFR PEFINRIDDI VVFHPLAMEQ IKSIARIQLQ
GLMARLEDKG FMVTISDSLL EQLTEAGFDP LFGARPLKRA IQQKVENPLA QAILSGKVTP
GKALMLDADE HGLVFKQEP
//
