ID A0A0X8GL10_9BURK Unreviewed; 878 AA.
AC A0A0X8GL10;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:AMC34106.1};
GN ORFNames=VN23_05600 {ECO:0000313|EMBL:AMC34106.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC34106.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC34106.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC34106.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014222; AMC34106.1; -; Genomic_DNA.
DR RefSeq; WP_046350043.1; NZ_CP014222.1.
DR AlphaFoldDB; A0A0X8GL10; -.
DR STRING; 1236179.VN23_05600; -.
DR KEGG; jab:VN23_05600; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000069577; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..155
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 157..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..83
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 439..486
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 878 AA; 95319 MW; 64F1517651A4FAB2 CRC64;
MSTPLKALIS RLTPTARRAV EEAASRALSR THFEIEIEHV VLAILAQDDN AGVAALHSLG
LSLDQLEKEL DAALDRFRTG NTRNPVLSTW LPKWLEKAWM LASVELGQDS VSTLDLLLAL
VQDDALRATL QGSSATLAKM DGKRALQGYV ALRQHGNEAA TSSENLPSDE APDMNLDQPA
PRRGSPGLDK YTIDLTAQAR LGKIDPVLGR ETEIRQMIDI LQRRRQNNPI LTGEPGVGKT
AVVEGLALKI VSGEVPPVLS GVTLRTLDLG LLQAGASVKG EFENRLRQVI DEVKASPVPI
ILFIDEAHTL IGAGGAAGQN DAANLLKPAL ARGELRTIAA TTWAEYKKYF EKDAALARRF
QVVKVDEPAP EIAVQMVRGL TDAMATHHEV VIMNEAVVAA VHLSSRYITG RQLPDKAISV
LDTACARVAL SRSGRPAPIE NVEVLIANIE REIKALQTEE GHGERIAELT GQREILEGDL
QQLQSAWAVQ QQVINEIEAL KAAAADAKPA KGKKVSPLQA KRTSLRELQK QHQLAYECVD
ESVIADVISG WTGIPLGRMV SNELVQVQKL ASLLAERVIG QDHALEQIAE RVQIAKANLD
DPSKPKGVFM LVGPSGVGKT ETALALAESL YGGERNLITI NMSEYQEAHS VSGLKGSPPG
YVGYGEGGVL TEAVRRKPYS VVLLDEVEKA HPDVMELFFQ VFDKGLLEDS EGREVDFKNT
IILLTSNTGT DLLMRACEHG VTVEDVTRDP TADDLIEILR PTLQKAFKPA FLGRLTIVPY
FPISDEVLRK IVALKLAKIA RRIAQNHGAV LEYPSELVES IANRCMDVDS GARDADAILT
RTVLAQISTD LLARMSVGKP VKKIVLSLKN DEVKVKIS
//