GenomeNet

Database: UniProt
Entry: F5Y187_RAMTT
LinkDB: F5Y187_RAMTT
Original site: F5Y187_RAMTT 
ID   F5Y187_RAMTT            Unreviewed;       874 AA.
AC   F5Y187;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 75.
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:AEG93488.1};
GN   OrderedLocusNames=Rta_23900 {ECO:0000313|EMBL:AEG93488.1};
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS   TTB310).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG93488.1, ECO:0000313|Proteomes:UP000008385};
RN   [1] {ECO:0000313|EMBL:AEG93488.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTB310 {ECO:0000313|EMBL:AEG93488.1};
RX   PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA   De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA   Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA   Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA   Vermeglio A., Achouak W., Heulin T.;
RT   "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT   Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL   PLoS ONE 6:E23784-E23784(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; CP000245; AEG93488.1; -; Genomic_DNA.
DR   RefSeq; WP_013901720.1; NC_015677.1.
DR   AlphaFoldDB; F5Y187; -.
DR   STRING; 365046.Rta_23900; -.
DR   KEGG; rta:Rta_23900; -.
DR   PATRIC; fig|365046.3.peg.2448; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_4; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008385; 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:UP000008385};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251};
KW   Stress response {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000313|EMBL:AEG93488.1}.
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   874 AA;  96954 MW;  4D57D26DD0CB6202 CRC64;
     MRLDKLTTKF QEALAEAQSL ALGNDHGYIE PEHLLVAMLR QEDGPRALLQ RAGVNIPGLQ
     AAAEAAMHKR PQVQGQEQVQ VGRDLVSLLQ AAEKEGIKRG DQFIASELFL LALADSKQDI
     GRIARANGLS RKSFEAAIAA VRGGSSVNSA EAEGQREALK KYCLDLTERA RLGKLDPVIG
     RDEEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVAGEVPESL KNKRVLSLDM
     AALLAGAKYR GEFEERLKSV LTELAKDEGQ TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
     LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPT VEATIAILRG LQEKYEAHHG
     VDITDPAIVA AAELSHRYIT DRFLPDKAID LIDEAASKIK IEIDSKPEAI DRLDRRMIQL
     QIEREAMRKE TDEASQKRLA LIEDEIAKLR KEIADLEDIW KAEKAAAQGS AQIREEMDRV
     RFQIEEFKRK ADFNKVAELQ YGRLPELERK LKEAQDAEAG KAKAGKAQLL RTQVGAEEIA
     EVVARATGIP VSKLMQGERE KLLQMEERLH QRVVGQDEAI AAVANAIRRS RSGLADPNRP
     TGSFLFLGPT GVGKTELCKA LATFLFDSEE HLIRVDMSEF MEKHSVARLI GAPPGYVGYE
     EGGYLTEAVR RKPYSVILLD EVEKAHHDVF NVLLQVLDDG RLTDGQGRTV DFKNTVIVMT
     SNIGSHMIQA MVGRPYEDVK EAVWDELKNH FRPEFLNRID ETVVFHGLHA AHIARIARIQ
     LGVLEQRLAK MDLTLQVSEA ALEELAKVGF DPVFGARPLK RAIQQRIENP LSRLILEGRF
     PPKSVIPVEV DPVREPGVFR FGDPKPQPAE EAVA
//
DBGET integrated database retrieval system