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Database: UniProt
Entry: A0A437JT88_9BURK
LinkDB: A0A437JT88_9BURK
Original site: A0A437JT88_9BURK 
ID   A0A437JT88_9BURK        Unreviewed;       869 AA.
AC   A0A437JT88;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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:RVT50380.1};
GN   ORFNames=ENE75_15290 {ECO:0000313|EMBL:RVT50380.1};
OS   Rubrivivax albus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=2499835 {ECO:0000313|EMBL:RVT50380.1, ECO:0000313|Proteomes:UP000288178};
RN   [1] {ECO:0000313|EMBL:RVT50380.1, ECO:0000313|Proteomes:UP000288178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICH-3 {ECO:0000313|EMBL:RVT50380.1,
RC   ECO:0000313|Proteomes:UP000288178};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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|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:RVT50380.1}.
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DR   EMBL; SACT01000005; RVT50380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437JT88; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000288178; 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 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288178};
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   869 AA;  95774 MW;  70E1095EB38CE46F CRC64;
     MRFDKLTTAF QQALGDAQSL AVARDNPYIE PAHLLAAMLQ QPDGPKALLD RAGANTAALK
     TAMETAIGGF PSVQVSGGQP VQPSRDLVTL LQAADKEASK RGDQFIASEM FLLAAADAKS
     DFGGILRGHG LTRKALEAAI DAVRGGQTVD SAEAEGQREA LKKYTLDLTE RARHGKLDPV
     IGRDDEIRRA IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPD SLREKRVLVL
     DMAGLLAGAK YRGEFEERLK AVLKEVAADE GRIILFIDEI HTMVGAGKAE GAIDAGNMLK
     PALARGELHC IGATTLNEYR KYVEKDAALE RRFQKVLVDE PTVEATVAIL RGLQEKYEVH
     HGVEITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAK IKIEIDSKPE AMDKLDRRLI
     QLKIEREAVR KEKDEASIKR MGLIEEEIAK LEREAADLEE IWKSEKAQAQ GSAQVKEEID
     RARQQIEELK RKGDFNAVAE LQYGKLPELE KRLHEAQAKE TGKKEAGKDG KAGPQLLRTM
     VGAEEIAEVV SRATGIPVSK LMQGERDKLL QMESKLHERV VGQDEAIVAV ADAIRRSRAG
     LSDPNRPLGS FLFLGPTGVG KTELCKALAG FLFDSEDHMV RIDMSEFMEK HSVSRLIGAP
     PGYVGYDEGG YLTEAVRRKP YSVLLLDEVE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFK
     NTVIVMTSNL GSHVIMQMAG QPSEDIKEAV WAEVKQHFRP EFLNRIDETV VFHALDQAHI
     ENIAKIQLKH LEQRLAKMEM KLEVSPEALA ELAKAGFDPV FGARPLKRAI QHRIENPVSK
     LILQGRFGPK DVIPVDVEGG QFVFERTVH
//
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