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Database: UniProt
Entry: A0A3D8PHE0_9RHOB
LinkDB: A0A3D8PHE0_9RHOB
Original site: A0A3D8PHE0_9RHOB 
ID   A0A3D8PHE0_9RHOB        Unreviewed;       875 AA.
AC   A0A3D8PHE0;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-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:RDW14639.1};
GN   ORFNames=DIE28_01915 {ECO:0000313|EMBL:RDW14639.1};
OS   Paracoccus thiocyanatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=34006 {ECO:0000313|EMBL:RDW14639.1, ECO:0000313|Proteomes:UP000256679};
RN   [1] {ECO:0000313|EMBL:RDW14639.1, ECO:0000313|Proteomes:UP000256679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SST {ECO:0000313|EMBL:RDW14639.1,
RC   ECO:0000313|Proteomes:UP000256679};
RA   Ghosh W., Rameez M.J., Roy C.;
RT   "Whole genome sequencing of Paracoccus thiocyanatus SST.";
RL   Submitted (MAY-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|ARBA:ARBA00004496,
CC       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:RDW14639.1}.
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DR   EMBL; QFCQ01000005; RDW14639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8PHE0; -.
DR   Proteomes; UP000256679; 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:UP000256679};
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   875 AA;  96021 MW;  B682D45E13E5288A CRC64;
     MDMEKFTERS RGFLQAAQTI AIREENQRVM PEHLLKALMD DDQGFASNLI ARAGGDAQAV
     RQAVDQAVAK QPKVSGGQGQ VYVDPSMVRV LDEAEKLAKK AGDSFVPAER VLTALAIVNT
     NARDALAAGK VTAQGLNSAI NDIRKGRTAD TASAEDSYEA LSKYARNLTE AAAEGKIDPI
     IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVDGDVPE SLRNKQLWAL
     DMGALIAGAK YRGEFEERLK SVLKEIENAA GEVVLFIDEL HVLVGAGKTD GAMDAANLIK
     PALARGELHC VGATTLDEYR KYIEKDAALA RRFQPVMVEE PTVEDTISIL RGIKEKYELH
     HGVRISDAAL VAAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDQLDRQIL
     QMQIEAEALK KEDDAASQDR LEKLEKQLSE LQEKSASLTA RWQAERDKLE GSRTLKERLD
     RARAELDQAK REGNLARAGE LSYGIIPGLE RQLAEAEGHN DGLLVEETVR PEQIAEVVER
     WTGIPTSKML EGEREKLLKM EDVLGNRVIG QSEAVTAVSN AVRRARAGLN DPKRPLGSFL
     FLGPTGVGKT ELTKAIAEYL FDDDSAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
     TEAVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGQLTDG QGRTVDFKQT LIVLTSNLGA
     QALSALPEGA DSGQARTQVM DAVRAHFRPE FLNRLDEIVI FHRLTRENMD AIVRIQLAQL
     EGRLAQHKIG LELDKPALKW LADEGYDPVF GARPLKRVMQ RSLQNPLAEM ILAGEVLDGH
     AVHVTAGPEG LVVGNRVSSA HLGSADESGP RVPLH
//
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