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Database: UniProt
Entry: A0A1M7GBE7_9RHOB
LinkDB: A0A1M7GBE7_9RHOB
Original site: A0A1M7GBE7_9RHOB 
ID   A0A1M7GBE7_9RHOB        Unreviewed;       876 AA.
AC   A0A1M7GBE7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05444389_1045 {ECO:0000313|EMBL:SHM13209.1};
OS   Paracoccus solventivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=53463 {ECO:0000313|EMBL:SHM13209.1, ECO:0000313|Proteomes:UP000184444};
RN   [1] {ECO:0000313|EMBL:SHM13209.1, ECO:0000313|Proteomes:UP000184444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6637 {ECO:0000313|EMBL:SHM13209.1,
RC   ECO:0000313|Proteomes:UP000184444};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FRCK01000004; SHM13209.1; -; Genomic_DNA.
DR   RefSeq; WP_073064868.1; NZ_FRCK01000004.1.
DR   AlphaFoldDB; A0A1M7GBE7; -.
DR   STRING; 53463.SAMN05444389_1045; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000184444; 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:SHM13209.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHM13209.1};
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..499
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   876 AA;  95977 MW;  4D1726089D31755C CRC64;
     MDMEKFTERS RGFLQAAQTI AIREENQRVV PEHLLKALMD DDQGLAANLI TRAGGDAQAV
     RRAVDEAVAR LPKVSGGDGQ VYVDSSLVRV MDEAQKIAKQ AGDSFVPVER VLMALAMVNT
     RARDALSAGQ VTTQALNAAI NDIRKGRTAD SASAEDTFEA LSKYARDLTA DAEQGRIDPI
     IGRDEEIRRT MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLANKKLMAL
     DMGALIAGAK YRGEFEERLK SVLKEVETAA GEIILFIDEL HVLVGAGKTD GAMDAANLIK
     PALARGELHC VGATTLDEYR KYIEKDAALA RRFQPVMVQE PTVEDTISIL RGIKEKYELH
     HGVRISDAAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDRQIL
     QMQIEAEALK KEDDAASRDR LERLEKQLSD LQQQSAELTA RWQAERDKLE GSRNVKEQLD
     RARAELEQAK REGNLARAGE LSYGIIPSLE RQIAETEGEG DGPLVEEAVR PEQIAEVVER
     WTGIPTSKLM EGERDKLLKM EEVLGQRVIG QSEAVTAVAN AVRRARAGLN DPRRPLGSFL
     FLGPTGVGKT ELTKAIAEYM FDDDSAMVRI DMSEFMEKHS VSRLIGAPPG YVGYDEGGVL
     TEAIRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGQLTDG QGRTVDFKNT LIILTSNLGA
     QALSSLPEGA DSGQARSEVM AAVRAHFRPE FLNRLDEIII FHRLSRDNMD AIVRIQLADL
     EKRLADRKIT LDLDEAAQTW LADEGYDPVF GARPLKRVIQ RSLQNPLAEM LLGGEVLDGQ
     TVHVTAGEGG LVVGNRVGTN APLGAAGDKP AGAPLH
//
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