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Database: UniProt
Entry: A0A1H1ESR7_9GAMM
LinkDB: A0A1H1ESR7_9GAMM
Original site: A0A1H1ESR7_9GAMM 
ID   A0A1H1ESR7_9GAMM        Unreviewed;       866 AA.
AC   A0A1H1ESR7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05216569_2548 {ECO:0000313|EMBL:SDQ91670.1};
OS   Pseudoxanthomonas sp. CF125.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ91670.1, ECO:0000313|Proteomes:UP000199049};
RN   [1] {ECO:0000313|EMBL:SDQ91670.1, ECO:0000313|Proteomes:UP000199049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF125 {ECO:0000313|EMBL:SDQ91670.1,
RC   ECO:0000313|Proteomes:UP000199049};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNLD01000002; SDQ91670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ESR7; -.
DR   STRING; 1855303.SAMN05216569_2548; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199049; 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; 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   Hydrolase {ECO:0000313|EMBL:SDQ91670.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDQ91670.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199049};
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   866 AA;  96142 MW;  FD4E83CD29AE1769 CRC64;
     MRMDKLTSRF QQALADAQSL AVGRDHNMIE PVHVLTALLD QSDGSTRPLL AQAGVNVPVL
     RERLTEALDK LPKVSGQAGN LSIGNDLTRL LNVTDKLAQQ HGDQFIASEW FVMAALEDKG
     ALGMALRAAG ADKAKLEAAI EKVRGGQSVQ SENAEEQRQA LEKYTIDLTE RAESGKLDPV
     IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKNRRVLSL
     DMGALIAGAK FRGEFEERLK AVLNDLSKTE GQVILFIDEL HTMVGAGKAE GSMDAGNMLK
     PALARGELHC IGATTLDEYR KYVEKDAALE RRFQKVFVGE PTVEDTIAIL RGLKERYAVH
     HGVEITDPAI VAAATLSHRY IADRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRKERRLI
     QLKIQREMLK KEKDSESQKR LADLEADIES LEREFSDLNE IWKSEKAALQ GSTRIKEQIE
     QARLDLEAAQ RHQDYARMSE IQYGLLPELE KQLQNAQEVD RKDFKLVQDR VTAEEIAEVV
     SRWTGIPVSK MLEGEREKLL KMESQLHTRV VGQEEAIKVV SDAMRRSRAG LSDPNRPTGS
     FLFLGPTGVG KTELCKALAE FLFDSSDAMI RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRRP YSLILLDEVE KAHSDVFNVL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
     GSHQIQDMSD NGGADVQSAE AYTQMKAAVM GVVQAHFRPE FINRLDDIVV FHPLDKAQIR
     EIARIQLKGL EKRLGERGLR IELEDSALQL LGNVGFDPVY GARPLKRAIQ QQLENPLAQK
     ILAGEFASGD TIRVGASGGG LVFTRG
//
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