ID A0A0Q5NW48_9BURK Unreviewed; 902 AA.
AC A0A0Q5NW48;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KQR78920.1};
GN ORFNames=ASG35_11220 {ECO:0000313|EMBL:KQR78920.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR78920.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR78920.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR78920.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR78920.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR78920.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQR78920.1}.
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DR EMBL; LMPF01000021; KQR78920.1; -; Genomic_DNA.
DR RefSeq; WP_056360652.1; NZ_LMPF01000021.1.
DR AlphaFoldDB; A0A0Q5NW48; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051826; Unassembled WGS sequence.
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:SF181; ATPASE SUBUNIT OF ATP-DEPENDENT PROTEASE-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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..157
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 464..498
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 902 AA; 98727 MW; 6C5E61CB6CDED59D CRC64;
MTARDLSPFL RRLNEHCARA LSDAASLCET RAHREIEIEH WLIKLLELGD GDLVAIARRY
ELEMDGIWNG LLKSIERLPH DLRGKPGLSQ RLGQILEAAW LRASLEEGQP AIRSAHLLAV
LADTPHFLRA PDAWQLLSVS AVQIERLMPE LDRVSVEAPK DASVKDTAAA VGPTEDLTPK
LQANSDALDR FTIDITQKAR DGKIDPVFGR DIEIRQMVDI LARRRKNNPI LVGEPGVGKT
ALVEGLALKI VEGDVPAIIR NVSILTLDLG LLQAGAGVKG EFEQRLKNVI EAVQASATPI
LLFIDEAHTL IGAGNTAGGA DAANLLKPAL ARGELRTIAA TTWSEYKQYF ERDAALERRF
QMVKVDEPDD DNACLMLRGL KERYAQHHGV HITDAAVGAA VRLSRRYLTG RQLPDKAVDL
LDTAAARVRM SIDATPVAIS TRRAEHAALE VERTALTHDQ GATSQEYGDR LAAIETRLET
LTRELVQLEV ELAQQKDAIH TLFDLRTQWH AATDESERRD VQAAIRHAHD QLSQHGSDAL
VYAEVDEAAI ARVIADWTGV PVGSLLSDEL ATLLELESRL GQVVVGQDDA LDALGKSLRA
AKAGLKSEEA PLGVFLLAGP SGVGKTETAR ALADLMFGGE RALVTINLSE YQEAHTVSQL
KGSPPGYVGY GQGGVLTEAV RRRPYSVILL DEVEKAHRDV LNVFYQVFDR GFMRDGEGRI
IDFRNTVIVM TSNLGSEQIM AAHDAVTEAV GDVTEVTEIT EITTSMLMEA IRPELIAHFQ
PALLARFQTV VYRPLSAEAM TTIVRMKLAK VAQRIERKFG LPLLCDDALI AELVRACHLP
DSGARNIDSL LDQQILPVLS RELLLRAAQE AKPDAVRLSY SDGDGIGVEF EMPTQSMVEA
AK
//