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Entry: A0A328ZB62_9BURK
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ID   A0A328ZB62_9BURK        Unreviewed;       869 AA.
AC   A0A328ZB62;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AX018_101692 {ECO:0000313|EMBL:RAR82884.1};
OS   Paracidovorax anthurii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=78229 {ECO:0000313|EMBL:RAR82884.1, ECO:0000313|Proteomes:UP000248856};
RN   [1] {ECO:0000313|EMBL:RAR82884.1, ECO:0000313|Proteomes:UP000248856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFPB 3232 {ECO:0000313|EMBL:RAR82884.1,
RC   ECO:0000313|Proteomes:UP000248856};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) 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:RAR82884.1}.
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DR   EMBL; QLTA01000016; RAR82884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328ZB62; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000248856; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:RAR82884.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RAR82884.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248856};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..490
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   869 AA;  95738 MW;  4DE9A99AACE99DB9 CRC64;
     MRLDKLTTKF QEALADAQSL ALGNDNAYIE PVHLLAAMLR QEDGPRALLQ RAGANAAGLQ
     TAAENAIKRL PQVQGQDQVQ VGPELGRLLQ ATEKEAIKRG DQFIASELFL LALVDGKGDT
     AQLAREHGCT RKSLEAAIDA VRGGAQVNSA EAEGQREALK KYTLDLTERA RAGKLDPVIG
     RDDEIRRAIQ VLQRRSKNNP VLIGEPGVGK TAIVEGLAQR IVAGEVPESL KDKRVLSLDM
     AALLAGAKYR GEFEERLKAV LNELAKDEGR TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
     LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPS VEATIAILRG LQERYELHHG
     VDITDPAIVA AAELSHRYIT DRFLPDKAID LIDEAAAKIK IEIDSKPEAI DKLDRRLIQL
     QIEREAVRRE KDEASQKRFA LIAEEIERLQ KEIADLEEIW TAEKAQAQGS AQVREEIERV
     KLQIVEFTRK GDLTKVSELQ YGRLPDLERK LKEAQAKEDG RDGASAPNRL LRTQVGAEEI
     AEVVSRATGI PVAKMLQGEK DKLLQMEGKL HERVVGQEEA IAAVANAIRR SRSGLADPNR
     PMGSFLFLGP TGVGKTELCK ALAGFLFDSE EHLVRIDMSE FMEKHSVARL IGAPPGYVGY
     EEGGYLTEAV RRKPYSVLLL DEVEKAHPDV FNVLLQVLDD GRLTDGQGRT VDFKNTVIVM
     TSNIGSHLIQ AMVGQDADDI KEAVWAELKN HFRPEFLNRI DETVVFHALD AKNIEAIARI
     QLHLLEARLA KMDLHLQVSP AALSELAKVG FDPVFGARPL KRAIQQRIEN PLSKLLLEGR
     FPPKSVIPVN VDPVQDPGVF RFGEPAAAG
//
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