ID H2G1U6_OCESG Unreviewed; 857 AA.
AC H2G1U6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=GU3_04905 {ECO:0000313|EMBL:AEY00738.1};
OS Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanimonas.
OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY00738.1, ECO:0000313|Proteomes:UP000007742};
RN [1] {ECO:0000313|EMBL:AEY00738.1, ECO:0000313|Proteomes:UP000007742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GK1 {ECO:0000313|EMBL:AEY00738.1,
RC ECO:0000313|Proteomes:UP000007742};
RX PubMed=22461556; DOI=10.1128/JB.00023-12;
RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT from Gavkhouni Wetland in Iran.";
RL J. Bacteriol. 194:2123-2124(2012).
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; CP003171; AEY00738.1; -; Genomic_DNA.
DR RefSeq; WP_014291470.1; NC_016745.1.
DR AlphaFoldDB; H2G1U6; -.
DR STRING; 511062.GU3_04905; -.
DR KEGG; oce:GU3_04905; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000007742; 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: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; 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 Hydrolase {ECO:0000313|EMBL:AEY00738.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AEY00738.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007742};
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 857 AA; 95799 MW; ADDB441CC48F4ACB CRC64;
MRLDRLTSKF QLALQDAQSM ALGRDHAYIE PAHLLVAMLN QEGGTIRPLL TTARVDGNAL
RVELDKSLDR LPRVSGGDMD VQVSPVLGRL LNQCDKLAQQ RKDAYISSEL FLLASLDDKG
ELGELLKRVG LSKDKLTKAI DDIRGGQKVD DPNAEENRQA LEKYTIDLTE RAEQGKLDPV
IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINGEVPE GLKNKRVLSL
DMGALVAGAK YRGEFEERLK ALLNELAKEE GRVILFIDEL HTMVGAGKGE GAMDAGNMLK
PALARGELHC VGATTLDEYR QYVEKDAALE RRFQKVLVDQ PTVEDTIAIL RGLKERYELH
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRLQIDSKPE PLDRLDRRII
QLKLEEQALL KEDDEGSRKR LQLIRDELAE KEKEYAELEE VWKSEKAALA GTQHIKAELE
QVRQELEVAR RASDLARMSE LQYGRIPELE KQLDLAAQAE MQEQHLLKNR VTDEEIADVL
SRWTGIPVAK MLEGEKEKLL RMEDSLHEQV IGQNEAVDAV ANAIRRSRAG LSDPNRPVGS
FLFMGPTGVG KTELCKALAD FLFDSRDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNI
GSDLIQEHSA SKDYDQMKAM LMEVLGHQFR PEFINRIDEI VVFHPLAQDQ IKAIARIQLQ
GLVERLESMD YQVSISDALL EKLATAGFDP LFGARPLKRA IQQKVEDPLA QAMLSGRVVP
GKLLKLDADD NGLVLNQ
//
