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Database: UniProt
Entry: A0A344PHW4_9RHOB
LinkDB: A0A344PHW4_9RHOB
Original site: A0A344PHW4_9RHOB 
ID   A0A344PHW4_9RHOB        Unreviewed;       876 AA.
AC   A0A344PHW4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-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   ECO:0000313|EMBL:AXC48969.1};
GN   ORFNames=DRW48_03960 {ECO:0000313|EMBL:AXC48969.1};
OS   Paracoccus suum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2259340 {ECO:0000313|EMBL:AXC48969.1, ECO:0000313|Proteomes:UP000252023};
RN   [1] {ECO:0000313|Proteomes:UP000252023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2-6 {ECO:0000313|Proteomes:UP000252023};
RA   Heo J., Kim S.-J., Kwon S.-W.;
RT   "Genome sequencing of Paracoccus sp. SC2-6.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP030918; AXC48969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344PHW4; -.
DR   KEGG; pars:DRW48_03960; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000252023; Chromosome.
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:UP000252023};
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   876 AA;  96259 MW;  A766490DE360294E CRC64;
     MDMEKFTERS RGFIQAAQTI AIRENNQRVM PEHLLKALMD DDQGLAANLI TRAGGNARAV
     ADAVTTAVDK LPKVQGGEGQ VYIDTSLVRV LDEAEKIAKK AGDSFVPVER ILMALTMVNT
     RARDALEAGK VTAQALNAAI NDVRKGRTAD SASSEDTMEA LSKYARDLTA AAAEGKIDPI
     IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVDGDVPE SLRNKKLMAL
     DMGALIAGAK YRGEFEERLK AILKEIESAN GEIILFIDEL HVLVGAGKTD GAMDAANLIK
     PALARGELHC VGATTLDEYR KYIEKDAALA RRFQPVMVEE PTVQDTISIL RGIKEKYELH
     HGVRITDSAL VAAATLSNRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDQLDRQIL
     QLQIEAEALK KEDDAASKDR LGRLERDLSD LQERSAEMTA RWQAERDKLE GTRGLKEQLD
     RARAELDQAK REGNLRKAGE LSYGIIPGLE KKLADSEGSD EGPMVEEAVR PEQIAEVVER
     WTGIPTTKML EGERDKLLQM EQVLARRVLG QNEAVTAIAN SVRRARAGLN DPHRPLGSFL
     FLGPTGVGKT ELTKAIAEYM FDDDDAMTRI DMSEFMEKHA VSRLIGAPPG YVGYDEGGVL
     TESVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGILTDG QGRRVDFKNT LIILTSNLGA
     QALSTLPEGS DSSDAREQVM AAVRAHFRPE FLNRLDEILI FRRLTRENMS GIVKLQLLGL
     ESRLADRNIH LDLDAQALKW LADEGYDPVY GARPLKRVIQ RSLQNPLAEM LLSGAVLDGE
     TVPITAGPEG LIVGNRVGKN APLGSAGDRP AGVPLQ
//
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