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Database: UniProt
Entry: A0A1Y0I384_9GAMM
LinkDB: A0A1Y0I384_9GAMM
Original site: A0A1Y0I384_9GAMM 
ID   A0A1Y0I384_9GAMM        Unreviewed;       863 AA.
AC   A0A1Y0I384;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=OLMES_0840 {ECO:0000313|EMBL:ARU54932.1};
OS   Oleiphilus messinensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oleiphilaceae; Oleiphilus.
OX   NCBI_TaxID=141451 {ECO:0000313|EMBL:ARU54932.1, ECO:0000313|Proteomes:UP000196027};
RN   [1] {ECO:0000313|EMBL:ARU54932.1, ECO:0000313|Proteomes:UP000196027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ME102 {ECO:0000313|EMBL:ARU54932.1,
RC   ECO:0000313|Proteomes:UP000196027};
RA   Kozyavkin S.A., Slesarev A.I., Golyshin P.N., Korzhenkov A.,
RA   Golyshina O.N., Toshchakov S.V.;
RT   "Genomic insights into alkan degradation activity of Oleiphilus
RT   messinensis.";
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; CP021425; ARU54932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0I384; -.
DR   KEGG; ome:OLMES_0840; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000196027; 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 104; 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:UP000196027};
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..439
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  96166 MW;  852E2102584D7C93 CRC64;
     MRIDKLTSRL QLALADSQSL ALGKDHNFIE PLHLMYVMLD QKGSSLNPLL KQLGVDVSAL
     KKQVAQKVDD LPIVKGNDGD VHMSNELGRL FNIADKLAQK RQDQYISSEL ILLAALEDRG
     ALGELLRQTG VQKEMLERAI DAIRGGEKVT DQGAEENRQA LDKYTIDLTA RATEGKLDPV
     IGRDDEIRRT IQVLQRRRKN NPVLIGDPGV GKTAIVEGLA QRIVNGEVPD GLKDKRVLSL
     DMGSLIAGAK FRGEFEERLK AVLNELAKQE GQIILFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLDEYR EFIEKDAALE RRFQKVLVEE PDEQATVAIL RGLKERYEVH
     HGVEITDGAI IAAAKLSHRY ITDRQLPDKA IDLVDEAASQ IRMEMDSKPE ALDKLERRLI
     QLKIEREALK KEADAASKQR LLDLDSVIAG IEQEYADLEE IWTTEKAALH GSQKIKSDLE
     QARVDLEAAH RAGDLARMSE LQYGRIPELE RQLDMASQAE MMEMKLLRNR VTDEEIAEVV
     SKWTGIPVAR MLEGEREKLL RMEEALHDRV IGQDEAVTVV ADAVRRSRAG LADPNRPNGS
     FLFLGPTGVG KTELCKSLAE FLFDTEDAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVLLLDEVE KAHPDVFNIL LQVLEDGRLT DGQGRTVDFK NTVVVMTSNL
     GSDVIQQFTR DESQYESMKA AVMDVVGGHF RPEFVNRIDE VVVFHPLRSE QIAGIAKIQL
     EILNQRLADQ DIALSVSDAA MSKLAEVGYD PVYGARPLKR AIQRWVENPL AQSILSGRFG
     RGDVIEAEVE GDGFRFERIQ AKH
//
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