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Database: UniProt
Entry: A0A165QZ57_9SPHN
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Original site: A0A165QZ57_9SPHN 
ID   A0A165QZ57_9SPHN        Unreviewed;       859 AA.
AC   A0A165QZ57;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=A3736_06360 {ECO:0000313|EMBL:KZY57149.1};
OS   Erythrobacter sp. HI0063.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY57149.1, ECO:0000313|Proteomes:UP000077326};
RN   [1] {ECO:0000313|EMBL:KZY57149.1, ECO:0000313|Proteomes:UP000077326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI0063 {ECO:0000313|EMBL:KZY57149.1,
RC   ECO:0000313|Proteomes:UP000077326};
RA   Sosa O.A.;
RT   "Microbial cycling of marine high molecular weight dissolved organic
RT   matter.";
RL   Submitted (MAR-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. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:KZY57149.1}.
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DR   EMBL; LWFF01000110; KZY57149.1; -; Genomic_DNA.
DR   RefSeq; WP_067679905.1; NZ_LWFF01000110.1.
DR   AlphaFoldDB; A0A165QZ57; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000077326; 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: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:UP000077326};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          415..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  94870 MW;  E2E9BD73B451BCFF CRC64;
     MNLEKFTDRA KGFLQAAQTV AIRMNHQRIS PAHLLKAMIE DSEGMASGLI ARAGGQPRMV
     EDDLDAALAK TPAVTGGGAQ ATPGLDNDAV RVLDQAEQIA QKSGDSYVTV ERLLVALALA
     TTTSAGQALK AGQVDPAKLE AAITELRGGR RADSANAEQA YDAMEKYARD LTQAARDGKL
     DPVIGRDEEI RRTVQILARR TKNNPALIGE PGTGKTAIAE GLALRIANGD VPDSLKNRTL
     MSLDLGALIA GAKYRGEFEE RLKAVLDEVK GADGQIILFI DEMHTLIGAG ASEGSMDAGN
     LLKPALSRGE LHCIGATTLD EYQKYVEKDP ALQRRFQPVY IEEPSVEDTI SILRGIKEKY
     ELHHGVRITD GAIVAAAQLS NRYIQNRFLP DKAIDLMDEA ASRIRMEVES KPEEIEGLDR
     RIIQLKIEEQ ALQKESDTAS RDRLEALRKE LSELEQQSSE LTTRWQNERD KIHAEARIKE
     ELDAARLELE QAQRAGDLAK AGELSYGRIP ELEKKLDEAS GQTENALLRE EVTEDDIAGV
     VSRWTGIPMD RMLEGEREKL LQMEEILGKR VIGQSQAIDA VSKAVRRARA GLQDPNRPLG
     SFLFLGPTGV GKTELTKALA RFLFDDDQAM VRIDMSEFME KHAVARLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHSDVFNV LLQVLDDGRL TDGQGRVVDF SNTLIILTSN
     LGSQFLAQMT DDQQVEDVEP QVMDVVRGHF RPEFLNRLDE IILFHRLGQD HMAPIVEIQV
     VRVQKLLKDR KITLDLTDAA KRWLGRVGYD PVYGARPLKR AVQRYVQDPL ADKMLRGEVP
     DGSSVRIDEG DGALEMAVE
//
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