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Database: UniProt
Entry: A0A3N7HN31_9BURK
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ID   A0A3N7HN31_9BURK        Unreviewed;       862 AA.
AC   A0A3N7HN31;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-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:RQP23544.1};
GN   ORFNames=DZC73_15445 {ECO:0000313|EMBL:RQP23544.1};
OS   Albitalea terrae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Albitalea.
OX   NCBI_TaxID=2496871 {ECO:0000313|EMBL:RQP23544.1, ECO:0000313|Proteomes:UP000267464};
RN   [1] {ECO:0000313|EMBL:RQP23544.1, ECO:0000313|Proteomes:UP000267464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-16 {ECO:0000313|EMBL:RQP23544.1,
RC   ECO:0000313|Proteomes:UP000267464};
RA   Khan S.A., Jeon C.O., Chun B.H., Jeong S.E.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RQP23544.1, ECO:0000313|Proteomes:UP000267464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-16 {ECO:0000313|EMBL:RQP23544.1,
RC   ECO:0000313|Proteomes:UP000267464};
RA   Shunsuke S.S.;
RT   "Rhizobacter gummiphilus sp. nov., a rubber-degrading bacterium isolated
RT   from the soil of a botanical garden in Japan.";
RL   Submitted (DEC-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:RQP23544.1}.
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DR   EMBL; QUSW01000004; RQP23544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N7HN31; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000267464; 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:UP000267464};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..143
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          409..489
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  95367 MW;  23A00FE56C624AB2 CRC64;
     MRLDKLTTKF QEALADAQSL AVTRDNPYIE PVHVLAAMLA QTDGPKALLE RASVHVGKLQ
     AATEREIEKL PQVQGGEQVQ PGRDLGALLQ ATEKEASKRG DQFIASELFL LAAADSKALG
     PLLKEHGLTR KSLETAIDAV RGGQKVDSAE AEGQREALKK YTLDLTERAR QGKLDPVIGR
     DDEIRRAIQV LQRRTKNNPV LIGEPGVGKT AIVEGLAQRI VAGEVPDSLK NKRVLVLDMA
     LLLAGAKFRG EFEERLKSVL KEVAQDEGQT IVFIDEIHTM VGAGKAEGAI DAGNMLKPAL
     ARGELHCIGA TTLDEYRKYL EKDAALERRF QKILVGEPSV EATIAILRGL QEKYEVHHGV
     EITDPAIVAA AELSHRYITD RFLPDKAIDL IDEAAAKIKI EIDSKPEAID KLDRRLIQLK
     IEREAVKREK DEASKKRLGL IEGEIERLTR EIADLEDLWK AEKAAAQGSA HVKEEIERIR
     IQIEDLKRKG DFNKVAELQY GKLPELERTL KEAQAKESKK GSDPGRPQLL RTLVGSEEIA
     EVVARATGIP VSKLMQGERE KLLHMEGKLH ERVVGQDEAI TAVANAIRRS RSGLSDPNRP
     TGSFLFLGPT GVGKTELCKA LAAFLFDSEE HLIRIDMSEY MEKHSVSRLI GAPPGYVGYD
     EGGYLTEAVR RKPYSVLLLD EVEKAHPDVF NVLLQVLDDG RLTDGQGRTV DFKNTVIVMT
     SNLGSHQIMQ MAGQDSEAIR DAVWVEVKQH FRPEFLNRID ETVVFHALDE KNIEAIAKIQ
     LKVLESRLEK MEMKLDVSPQ ALAELAKAGF DPVFGARPLK RAIQQRIENP VSKLILEGKF
     GPKDVIPVGV EGGELVFART VH
//
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