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Database: UniProt
Entry: A0A3D9BUX3_9RHOB
LinkDB: A0A3D9BUX3_9RHOB
Original site: A0A3D9BUX3_9RHOB 
ID   A0A3D9BUX3_9RHOB        Unreviewed;       878 AA.
AC   A0A3D9BUX3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:REC57335.1};
GN   ORFNames=DRV84_07765 {ECO:0000313|EMBL:REC57335.1};
OS   Rhodosalinus sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodosalinus.
OX   NCBI_TaxID=1940533 {ECO:0000313|EMBL:REC57335.1, ECO:0000313|Proteomes:UP000257131};
RN   [1] {ECO:0000313|EMBL:REC57335.1, ECO:0000313|Proteomes:UP000257131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDN1C137 {ECO:0000313|EMBL:REC57335.1,
RC   ECO:0000313|Proteomes:UP000257131};
RX   PubMed=29043957; DOI=10.1099/ijsem.0.002424;
RA   Guo L.Y., Ling S.K., Li C.M., Chen G.J., Du Z.J.;
RT   "Rhodosalinus sediminis gen. nov., sp. nov., isolated from marine
RT   saltern.";
RL   Int. J. Syst. Evol. Microbiol. 67:5108-5113(2017).
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:REC57335.1}.
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DR   EMBL; QOHR01000007; REC57335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9BUX3; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000257131; 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:UP000257131};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..500
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   878 AA;  96723 MW;  463F41F458315FAD CRC64;
     MDLSKFTERS RGFMQAAQTI AVREGHQKLA PEHLLKALMD DEQGLAANLI RRAGGAPERV
     SEAVEAALAK VPQVSGSGAG QVYLDQQTAK VMDEAEKLAK KAGDSFVPVE RILTALGMVK
     SPAKEALEAG AVSPQKLNEA INDLRKGRTA DTESAEEGYD ALRKYARDLT EAAEEGRIDP
     IIGRDEEIRR AMQVLSRRTK NNPVLIGDPG VGKTAIAEGL ALRIVNGDVP ESLRDKKLLA
     LDMGALIAGA KYRGEFEERL KAVLSEITAA AGEIILFIDE MHTLVGAGKA DGAMDASNLL
     KPALARGELH CVGATTLDEY RKHVEKDAAL ARRFQPLYVD EPTMEDTVSI LRGIKEKYEL
     HHGVRISDSA LVAAAQLSDR YITDRFLPDK AIDLMDEAAS RLRMEVDSKP EELDQLDRQI
     LQMQIEAEAL KKEDDAASRD RLEKIEKELA ELQERSAEMT ARWQAERDKL ASARELKEQL
     DQARNELEQA KREGNLARAG ELSYGIIPQL ESQLAEAEAR EGEGETEDGV MVEEAVRPEQ
     IAAVVERWTG IPMSKMLEGE REKLLRMEEE LHARVVGQDQ AVTAVANAVR RARAGLNDEN
     RPLGSFLFLG PTGVGKTELT KSLADFLFDD ESAMVRIDMS EFMEKHSVAR LIGAPPGYVG
     YEEGGVLTEA VRRRPYQVVL FDEVEKAHPD VFNVLLQVLD DGMLTDGQGH HVDFKQTLIV
     LTSNLGSQAL SRLPEGADSS QAKGEVMEAV RNHFRPEFLN RLDEIIVFDR LERADMTGIV
     EIQLGELQKR LAARKIRLEM DEAAKEWLAN EGYDPVFGAR PLKRVIQKAL QDPLAEMLLG
     GEVKDGDVIP VSAGADGLLI GDRVGRSDRQ PPEEAVLH
//
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