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Database: UniProt
Entry: A0A2I0CSR0_9PSED
LinkDB: A0A2I0CSR0_9PSED
Original site: A0A2I0CSR0_9PSED 
ID   A0A2I0CSR0_9PSED        Unreviewed;       854 AA.
AC   A0A2I0CSR0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=CW360_05160 {ECO:0000313|EMBL:PKF72184.1};
OS   Pseudomonas pharmacofabricae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1905276 {ECO:0000313|EMBL:PKF72184.1, ECO:0000313|Proteomes:UP000242861};
RN   [1] {ECO:0000313|Proteomes:UP000242861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZYSR67-Z {ECO:0000313|Proteomes:UP000242861};
RA   Yu X.-Y.;
RL   Submitted (DEC-2017) 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. {ECO:0000256|RuleBase:RU362034}.
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:PKF72184.1}.
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DR   EMBL; PIYS01000005; PKF72184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0CSR0; -.
DR   Proteomes; UP000242861; 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:UP000242861};
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          405..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   854 AA;  95011 MW;  B53E299ACD376F82 CRC64;
     MRIDRLTSKL QLALSDAQSL AVGMDHPAIE PLHLLQALLE QQGGSIRPLL LQVGFDINGL
     RQALAKELDQ LPKIQNPTGD VNLSQDLARL LNQADRLAQQ KGDQFISSEL VLLAGMDENT
     RLGKLLLGQG VTKKALENAI ANLRGGEAVN DPNAEESRQA LDKYTVDLTK RAEDGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPD GLKDKRLLSL
     DMGALIAGAK FRGEFEERLK AVLNELGKQE GRVILFIDEL HTMVGAGKAE GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVLVDE PSEEDTIAIL RGLKERYEVH
     HKVTITDGAI IAAAKLSHRY ITDRQLPDKA IDLIDEAASR IRMEIDSKPE ELDRLERRLI
     QLKVEREALK KEDDEAALKR LEKLKEDIAR LEQEYADLEE IWKSEKAEVQ GSAQIQQKIE
     QAKADLEAAR RKGDLNRMAE LQYGIIPDLE RSLQMVDQHG KPENQLLRSK VTDEEIAEVV
     SKWTGIPVSK MLEGEREKLL KMEGLLHQRV IGQEEAVVAV SNAVRRSRAG LADPNRPSGS
     FLFLGPTGVG KTELCKALAE FLFDTEEALV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     YLTEAVRRKP YSVVLMDEVE KAHPDVFNVL LQVLEDGRLT DSHGRTVDFK NTVIVMTSNL
     GSAQIQELVG DREAQRAAVM DAVSGHFRPE FINRIDEVVV FEPLGREQIA GIAEIQLQRL
     RRRLAERELS LELTPQALDK LVAVGYDPVY GARPLKRAIQ RWIENPLAQQ ILSGQFAPGA
     VVRAEVSGEE IIFA
//
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