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Database: UniProt
Entry: A0A0G4JWN6_9GAMM
LinkDB: A0A0G4JWN6_9GAMM
Original site: A0A0G4JWN6_9GAMM 
ID   A0A0G4JWN6_9GAMM        Unreviewed;       824 AA.
AC   A0A0G4JWN6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BN1221_02767 {ECO:0000313|EMBL:CPR17658.1};
OS   Brenneria goodwinii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=1109412 {ECO:0000313|EMBL:CPR17658.1, ECO:0000313|Proteomes:UP000044377};
RN   [1] {ECO:0000313|Proteomes:UP000044377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OBR1 {ECO:0000313|Proteomes:UP000044377};
RA   Paterson Steve;
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; CGIG01000001; CPR17658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4JWN6; -.
DR   STRING; 1109412.BN1221_02767; -.
DR   Proteomes; UP000044377; 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:UP000044377};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..113
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          379..459
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   824 AA;  91664 MW;  E82BF494081B6C0F CRC64;
     MMSALLNQEG GTVGPLLTAA GANVPHLKTE IDHAIARLPQ VEGTGGDVQP SSELVRTLNV
     CDKLAQKRGD TFISSELFVL AVLDSHSTLS DMIKNTGATQ ESVTKAIDQI RGGEQVNDQG
     AEDQRQALKK YTIDLTERAE QGKLDPVIGR DEEIRRTIQV LQRRTKNNPV LIGEPGVGKT
     AIVEGLALRI VNGEVPEGLK NKRVLSLDMG SLVAGAKYRG EFEERLKGVL TDLSKQEGSV
     ILFIDELHTM VGAGKADGAM DAGNMLKPAL ARGELHCVGA TTLDEYRQYV EKDAALERRF
     QKVFVAEPTV EDTIAILRGL KERYELHHHV QITDPAIVAA ATLSHRYIAD RKLPDKAIDL
     IDEAASSIRI QIDSKPEPLD RLDRRIIQLK LEQQALKKES DEASQKRLEL LNTELEEKER
     EYSKLEEEWK AEKASLTGTQ NIKAALEQAK ISLEQARRQG DLGQMSEIQY GKIPELEKQL
     AAATQLEGKT MHLLRNRVTD TEIAEVLARW TGIPVSRMLE SEREKLLRME EALHQRVIGQ
     DEAVEAVSNS IRRSRAGLSD PNRPIGSFLF LGPTGVGKTE LCKTLASFLF DSDDAMVRID
     MSEFMEKHSV SRLVGAPPGY VGYEEGGYLT EAVRRRPYSV ILLDEIEKAH PDVFNILLQV
     LDDGRLTDGQ GRTVDFRNTV VIMTSNLGSD LIQERFGERS YAEMRGMVLE VVSHSFRPEF
     INRIDEVVVF HPLGRKHISS IAKIQLQRLY KRLEERGYHV TITDAALERL GEIGFDPVYG
     ARPLKRAIQQ LIENPLAQQI LSGKLIPGKP VTLDVDGENI VARQ
//
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