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Database: UniProt
Entry: A0A208XES6_9BURK
LinkDB: A0A208XES6_9BURK
Original site: A0A208XES6_9BURK 
ID   A0A208XES6_9BURK        Unreviewed;       865 AA.
AC   A0A208XES6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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:OVZ54501.1};
GN   ORFNames=CDO44_26200 {ECO:0000313|EMBL:OVZ54501.1};
OS   Pigmentiphaga sp. NML080357.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pigmentiphaga.
OX   NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ54501.1, ECO:0000313|Proteomes:UP000196551};
RN   [1] {ECO:0000313|EMBL:OVZ54501.1, ECO:0000313|Proteomes:UP000196551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML080357 {ECO:0000313|EMBL:OVZ54501.1,
RC   ECO:0000313|Proteomes:UP000196551};
RA   Bernier A.-M., Bernard K.;
RT   "Pigmentiphaga species Genome sequencing and assembly.";
RL   Submitted (MAY-2017) 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:OVZ54501.1}.
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DR   EMBL; NINW01000057; OVZ54501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A208XES6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000196551; 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   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   865 AA;  96271 MW;  87BA1815F8F81F28 CRC64;
     MRIDRLTTKF QQALADAQSL AARNDNPYIE PLHVLAALLA DPESGAASLL ARAGVAVSKL
     TPEVNAAIGR LAQVQGSDAN IQVSRDLQGL FNKIDKEAAN RGDTYIASEL FLLALADDKG
     EAGRLLREAG LQRKALEAAI DAVRGGAPVD SQEGESNREA LKKYTLDLTE RARQGKLDPV
     IGRDDEIRRT IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNDEVPE TLKGKRVLSL
     DMAGLLAGAK FRGEFEERLK SVLKELSQEA GKNIVFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVDE PSVEATIAIL RGLQERYELH
     HGVDITDPAI VAAAELSNRY ITDRFLPDKA IDLIDEAAAR IRMEIDSKPE VMDKLDRRMI
     QLKIEREAVK KETDEASQRR LQLLEEELGK LEREYNDYEE VWKAEKAAVQ GAQSIKEEIE
     KVRAEMSELQ RKGQFDKLAE LQYGKLPELE ARLKSAEGKE KAAGKDRDKP KLLRTEVGAE
     EIAEVVSRAT GIPVSKMLQG ERAKLLHMEE KLHERVIGQD EAVRLVSDAI RRSRAGLSDP
     QRPYGSFLFL GPTGVGKTEL TKALAGFLFD SDDHMVRIDM SEFMEKHSVA RLIGAPPGYV
     GYEEGGYLTE AVRRKPYSVI LLDEVEKAHP DVFNVLLQVL DDGRLTDGQG RTVDFRNTVI
     VMTSNLASQQ IQAMAGQQYD VIKAVVWDEI KQHFRPEFLN RIDEVVVFHG LDAKHIESIA
     RVQLQRLAER LAKMDMRLEV SDDAIAQIAR AGFDPVFGAR PLKRAIQQEI ENPVAKLILE
     GKFGPKDVVP VDWNEGRFVF TRTLQ
//
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