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Database: UniProt
Entry: A0A0X8GL10_9BURK
LinkDB: A0A0X8GL10_9BURK
Original site: A0A0X8GL10_9BURK 
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
//
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