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
//