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Database: UniProt
Entry: J3HSQ8_9BURK
LinkDB: J3HSQ8_9BURK
Original site: J3HSQ8_9BURK 
ID   J3HSQ8_9BURK            Unreviewed;       794 AA.
AC   J3HSQ8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574};
DE   Flags: Fragment;
GN   ORFNames=PMI40_02489 {ECO:0000313|EMBL:EJN04711.1};
OS   Herbaspirillum sp. YR522.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJN04711.1, ECO:0000313|Proteomes:UP000007507};
RN   [1] {ECO:0000313|EMBL:EJN04711.1, ECO:0000313|Proteomes:UP000007507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR522 {ECO:0000313|EMBL:EJN04711.1,
RC   ECO:0000313|Proteomes:UP000007507};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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   -!- 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:EJN04711.1}.
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DR   EMBL; AKJA01000086; EJN04711.1; -; Genomic_DNA.
DR   RefSeq; WP_008115548.1; NZ_AKJA01000086.1.
DR   AlphaFoldDB; J3HSQ8; -.
DR   STRING; 1144342.PMI40_02489; -.
DR   PATRIC; fig|1144342.3.peg.2360; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000007507; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
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; 1.
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|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007507};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..77
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          343..423
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EJN04711.1"
SQ   SEQUENCE   794 AA;  87785 MW;  649F672741F155B4 CRC64;
     RLPQVSGNGG EVQVGRELVA LLNLADKQAQ QHGDQFVSSE MVLLGLVDDK SDAGRAARDN
     GLTRKSLEAA IVAVRGGASV SSQQDEGQRE ALKKYTLDLT ERARAGKLDP VIGRDDEIRR
     AIQVLQRRSK NNPVLIGEPG VGKTAIVEGL AQRIVNGEVP DSLKSKRVLS LDMAALLAGA
     KYRGEFEERL KSVLKEIAQD EGQTIVFIDE LHTMVGAGKA EGAMDAGNML KPALARGELH
     CVGATTLDEY RQYIEKDAAL ERRFQKILVD EPSVEATIAI LRGLQEKYEV HHGVDITDPA
     IVAAAELSHR YITDRFLPDK AIDLIDEAAA KIKIEIDSKP EVMDKLDRRL IQLKIEREAV
     KREKDEASQK RLQLIEEEIA RLDREYADLE EIWKAEKSTA QGGQQLREEI EKLRIQMEEA
     TRKSDWQKVS ELKYGKLAEL EAALEVQNKK DAAGVTGEKP RLVRTQVGAE EIAEIVARAT
     GIPVSRMMQG EREKLLHMEE VLHERVVGQD EAIIAVSDAI RRSRAGLGDP SKPYGSFMFL
     GPTGVGKTEL CKTLASYLFD TEEAIIRIDM SEFMEKHSVA RLIGAPPGYV GYEEGGHLTE
     AVRRKPYSVI LLDEIEKAHP DVFNVLLQVL DDGRMTDGQG RTVDFKNTVI VMTSNLGSHK
     IQSMEGSDPA LVKLAVMAEV RTHFRPEFIN RVDELVVFHA LDEKNIGAIA RIQLRILEQR
     LARLEIGLEI SDAALQKIAE AGFDPVYGAR PLKRAIQQEI ENPLSKAILG GSFGPKDVVH
     VGVENGQLSF TRDA
//
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