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Database: UniProt
Entry: A0A139BPL0_9PROT
LinkDB: A0A139BPL0_9PROT
Original site: A0A139BPL0_9PROT 
ID   A0A139BPL0_9PROT        Unreviewed;       859 AA.
AC   A0A139BPL0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AWT59_2970 {ECO:0000313|EMBL:KXS30909.1};
OS   Candidatus Gallionella acididurans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=1796491 {ECO:0000313|EMBL:KXS30909.1, ECO:0000313|Proteomes:UP000070578};
RN   [1] {ECO:0000313|EMBL:KXS30909.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS30909.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXS30909.1, ECO:0000313|Proteomes:UP000070578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ShG14-8 {ECO:0000313|EMBL:KXS30909.1};
RA   Kadnikov V., Ivasenko D., Beletsky A., Mardanov A., Danilova E.,
RA   Pimenov N., Karnachuk O., Ravin N.;
RT   "New uncultured bacterium of the family Gallionellaceae from acid mine
RT   drainage: description and reconstruction of genome based on metagenomic
RT   analysis of microbial community.";
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|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:KXS30909.1}.
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DR   EMBL; LSLI01000122; KXS30909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139BPL0; -.
DR   PATRIC; fig|1796491.3.peg.3255; -.
DR   Proteomes; UP000070578; 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:UP000070578};
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   859 AA;  95119 MW;  6A89163E2D0EFF2A CRC64;
     MRFDKFTTKF QQALSDAQSL AVGSDNQFIE PQHLLLALLN DADSGAASLL GRAGGNVVPL
     KAALKEAVER LAKVEGHGGE VQVGRDMSNL LNLTDKAAQK RGDEFIASEM FLLAACDDKG
     ETGRLLKQHG VARAPLEQAI TAVRGGETVG SQEAEGQRES LKKYTIDLTE RARQGKLDPV
     IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLKGKKVLSL
     DMAALLAGAK YRGEFEERLK NVLKELAQDE GQTIVFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVEE PSVEATIAIL RGLQERYELH
     HGVDITDPAI IAAAELSHRY ITDRFLPDKA IDLIDEAAAR VRMEIDSKPE VMDKLDRRLI
     QLKIEREAVK KEKDEASQKR FALIEEEIKK LQREYADLEE IWKAEKGAAQ GTAHLKEEME
     KVRAEIVQLQ RAGKLEQVAE LQYGKLPQLE AKLKEAVHAE ESKPKNRLLR TQVGAEEIAE
     VVSRATGIPV SKMMQGERDK LLKMEDKLHE RVVGQDEAVR LVSDAIRRSR SGLSDPNRPY
     GSFLFLGPTG VGKTELCKAL AGFMFDSEDH LIRIDMSEYM EKHSVARLIG APPGYVGYEE
     GGGLTEAVRR KPYSVILLDE VEKAHPDVFN VLLQALDDGR MTDGQGRTVD FKNTVIVMTS
     NLGSQMIQTM AGDDYQVIKL AVMGEVKSYF RPEFINRIDE VVVFHALDEK NIKSIARIQL
     KYLETRLAAM GMKLDISDAA LAEIANAGFD PVYGARPLKR AIQAQLENPL ARQILEGRFA
     AKDTIRVDCK GGVMKFDKA
//
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