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Database: UniProt
Entry: V4PBT5_9CAUL
LinkDB: V4PBT5_9CAUL
Original site: V4PBT5_9CAUL 
ID   V4PBT5_9CAUL            Unreviewed;       860 AA.
AC   V4PBT5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=ABENE_10235 {ECO:0000313|EMBL:ESQ91382.1};
OS   Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ91382.1, ECO:0000313|Proteomes:UP000017837};
RN   [1] {ECO:0000313|EMBL:ESQ91382.1, ECO:0000313|Proteomes:UP000017837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ91382.1,
RC   ECO:0000313|Proteomes:UP000017837};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ91382.1}.
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DR   EMBL; AWGB01000017; ESQ91382.1; -; Genomic_DNA.
DR   RefSeq; WP_018080795.1; NZ_AWGB01000017.1.
DR   AlphaFoldDB; V4PBT5; -.
DR   STRING; 1121022.GCA_000376105_01132; -.
DR   PATRIC; fig|1121022.4.peg.2067; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000017837; 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:UP000017837};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..490
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   860 AA;  94437 MW;  D8571695236E284C CRC64;
     MNIEKYSEKT QKLIQSAQGI AQARNHQYFS PIHVLKALTE DKESLSSQLI SLAGGRADAF
     AASVDLALGK LPAVTGGAQL YMANETNKLF NDAENDANKA GDSFVTADRL LIAAVDNKEG
     AEALKAAGIS LGKLKAAQAA FRKGKPADSA SAENGFDALK KYARDLTQAA LDGKIDPVIG
     RDEEIRRTIQ VLARRTKNNP VLIGEPGVGK TAIVEGLAQR IINGDVPESL KDKKLYSLDM
     GSLIAGAKYR GEFEERLKGV LNEVTQAEGQ IVLFIDEMHT LVGAGKGDGA MDASNLLKPA
     LARGELHCVG ATTLDEYRKH VEKDAALARR FQPVFVTEPT VEDTISILRG LKEKYEVHHG
     VRISDSAIVS AATLSNRYIA DRFLPDKAID LIDEAASRVR MAVDSKPEEL DELDRRIVQL
     KIEREALQKE TDAGSKTRLE KLSEELEDLE EKSLSLTTRW KAEKDKVGSA ARSREALERA
     RIDLANAQRA GDLQKASEIM YGIIPALEKA LERAENAPQG EQSPLTPEVV DSAQIAQVVS
     RWTGIPVDKM LEGERDKLLR MEDVLRGRVV GQDEALTAVA DAVRRARAGL KDPNRPIGSF
     LFLGPTGVGK TELNKALAEF LFDDETAITR LDMSEYMEKH SVSRMIGAPP GYVGYDEGGA
     LTEAVRRRPY QVVLFDEVEK AHPDVFNILL QVLDDGRLTD GQGRVVDFRN TLIVMTSNLG
     SDILVNIDDA TPVETVRPLV MEVVRRHFRP EFLNRIDETI LFHRLDKVHM HDIVRIQLKG
     LEKLMKDRDM TLSIDEAALT YLADKGYDPA YGARPLKRVI QKLLVDGIAR QILSGTVTDG
     DVIHVGFDGE ELAIGKPTVN
//
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