ID E3HRR3_ACHXA Unreviewed; 869 AA.
AC E3HRR3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Chaperone protein ClpB 3 {ECO:0000313|EMBL:ADP19682.1};
GN Name=clpB3 {ECO:0000313|EMBL:ADP19682.1};
GN OrderedLocusNames=AXYL_06389 {ECO:0000313|EMBL:ADP19682.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP19682.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP19682.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP19682.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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DR EMBL; CP002287; ADP19682.1; -; Genomic_DNA.
DR RefSeq; WP_013396969.1; NC_014640.1.
DR AlphaFoldDB; E3HRR3; -.
DR STRING; 762376.AXYL_06389; -.
DR KEGG; axy:AXYL_06389; -.
DR PATRIC; fig|762376.5.peg.6394; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_1_1_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000006876; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..156
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 869 AA; 93715 MW; 0A8F435A8AE1F67F CRC64;
MSDIGRIDLF GKLNPLLYQT LEGATAFCKL RGNPYVELVH WVHQILHAQD SDLHRIARRF
GLDMAALQAD LTAELDRLPA GAGSVSDLSE HIDHAVERAW VLGSLRYGAA RIRSAHLLAG
LARTYALRHV LLGMSAQFSR IVPDTLLEQL QEIVQGSPED AAEAASVAAA GAPGEGGSAL
ARFAVDLTAR ARAGEIDPVS GRDEEIRQLI DVLMRRRQNN PLLAGEAGVG KTAVVEGLAL
RLAAGEVPPQ LRDVALYLLD IGLLQAGAGV KGEFEQRLRG VIDEVQASER PVVLFIDEIH
TLVGAGGAAG TGDAANLLKP ALARGQLRTI GATTWSEYKK YIEKDPALSR RFQVVQVHEP
DEARAFGMLR GLAETLQAHH GVLLLDEAIE AAVTLSHRYI PARQLPDKAV ALLDTACARV
AVSQHAVPPS LEDARRRVQA LELAQRIAER ELRLGEGDAQ RIQRLAAEQA GAADDERTLA
ARWESERALA GHVLTLRKTL DLAASDAQED QRRALAQARV ALAASQGETA MVHCAVDAAA
VAAVVADWTG IPVGRMLRDE ARAVLDLADT LSTRVIGQRE ALEAVARRVQ TSRAGLTDPD
KPVGVFLLCG PSGVGKTETA LALAEALYGG EQNLITINMS EFQESHTVST LKGAPPGYVG
YGEGGVLTEA VRRRPYSVVL LDEVEKAHAD VHEIFFQVFD KGWMEDGEGR YIDFRNAVII
LTSNVGADRI AALCRDPELL PDSVALAAAL REQLLQAFPA ALLGRLVAVP YLPLPDTMLA
RIVDLQFERV RRRLSEHHGI VLEVTPEATA LVVARCAEVE SGARMVDAVL TNTVLPRISR
ELLGASMQDR RLSRVGLSAA DGEFRYDYA
//
