GenomeNet

Database: UniProt
Entry: G2J2A5_PSEUL
LinkDB: G2J2A5_PSEUL
Original site: G2J2A5_PSEUL 
ID   G2J2A5_PSEUL            Unreviewed;       858 AA.
AC   G2J2A5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
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:BAK76281.1};
GN   OrderedLocusNames=NH8B_1459 {ECO:0000313|EMBL:BAK76281.1};
OS   Pseudogulbenkiania sp. (strain NH8B).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK76281.1, ECO:0000313|Proteomes:UP000001274};
RN   [1] {ECO:0000313|Proteomes:UP000001274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX   PubMed=22038961; DOI=10.1128/JB.06127-11;
RA   Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT   "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT   Pseudogulbenkiania sp. strain NH8B.";
RL   J. Bacteriol. 193:6395-6396(2011).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP012224; BAK76281.1; -; Genomic_DNA.
DR   RefSeq; WP_014086665.1; NC_016002.1.
DR   AlphaFoldDB; G2J2A5; -.
DR   STRING; 748280.NH8B_1459; -.
DR   KEGG; pse:NH8B_1459; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_4; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000001274; 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:UP000001274};
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"
FT   COILED          774..801
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   858 AA;  94593 MW;  72EA41709EBC0231 CRC64;
     MRFDKLTTKF QQALADAQSL ALSHDHAYIE PQHLLAAMLD DADSGVGSLL ARAGVNVAGL
     RGGLKSAIDR LPKVQGTGGE ITVSRDLGNL LNLTDKAAMK RGDAFIASEL FLLALLDDKG
     ETGRQLKDNG GSANALNAAI DAVRGGANVE SQDAESQREA LKKYTLDLTE RARQGKLDPV
     IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLKHKKLLVL
     DLAALLAGAK YRGDFEERLK SVLSDLAKDE GNTLIFIDEI HTLVGAGKAE GAMDAGNMLK
     PALARGELHC LGATTLDEYR KYIEKDAALE RRFQKVLVDE PSVEDTIAIL RGLQEKYEIH
     HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAASR IKMELDSKPE EMDKLDRRLI
     QLKIEREAVK KESDEASQKR LGLIEDEIDR LSREYADLEE IWKAEKATAQ GSQSIKEEID
     RLKVEMEDLK RQGDWQKLAE LQYGKLPQLE ARLKEAEAAG AGTQKPNRLL RTQVGAEEIA
     EVVSRMTGIP VSKMLAGERE KLLKMEEVMH ERLVGQDEAV RAVSDAIRRS RSGLSDPNRP
     YGSFLFLGPT GVGKTELCKT LAGFLFDSED HLIRIDMSEY MEKHSVARLI GAPPGYVGYE
     EGGQLTEQVR RKPYSVILLD EVEKAHPEVF NILLQVLDDG RLTDGQGRTV DFKNTVVVMT
     SNIGSQHIQA MGSDDYQVIK LAVMAEVKGY FRPEFINRID EVVVFHALGS AQIRSIARIQ
     LKSLERRLAK LELSLQVTDA ALDAIAEAGF DPVYGARPLK RAIQSDIENP LAKAILAGKY
     EPKATVLVDA QNGQIVFE
//
DBGET integrated database retrieval system