ID A0A0Q8RTY8_9BURK Unreviewed; 892 AA.
AC A0A0Q8RTY8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KRC02725.1};
GN ORFNames=ASE26_16030 {ECO:0000313|EMBL:KRC02725.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRC02725.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRC02725.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRC02725.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC02725.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRC02725.1,
RC ECO:0000313|Proteomes:UP000051728};
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:KRC02725.1}.
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DR EMBL; LMIC01000002; KRC02725.1; -; Genomic_DNA.
DR RefSeq; WP_055936848.1; NZ_LMIC01000002.1.
DR AlphaFoldDB; A0A0Q8RTY8; -.
DR Proteomes; UP000051728; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000051728};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..175
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 448..499
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 892 AA; 96275 MW; 9CBF0F68ACDFB9BC CRC64;
MSINLKTLIG KLNDTCRNAA TRAASICVGL GQYEVDQEHL LLALLENPRS DMVALARHFE
VDTSRLQSDL QAEIARFRSG NARTPVFSAR LPKLFENAWL IASLDLQAGQ QVFIRSGHLL
QAMLTDPELS QLAYRSSALF HRFEADDIKH HLDKLTANSE EAEAAAATRA AVTGGEGGLG
GDPVGEMQQP AGKTPALDQF TTNLTERARA GKVDPVIGRD AEIRQAIDIL MRRRQNNPIL
TGEAGVGKTA VVEGLALRIA QGDVPDVLKG VAIHTLDMGL LQAGASVKGE FENRLKNVID
EVRKSPTPII LFIDEAHTMI GAGGQAGQND AANLLKPALA RGELRTIAAT TWGEYKKYFE
KDAALARRFQ VIKVEEPSEE LACAMLRGMA PLMEQHFNVR IFDEAITEAV RLSHRYIMGR
QLPDKAISVL DTACAKVALG QSATPALIES LQRRLERMAV ETGALERELA AGGAHQERLQ
ELAGLRGAAQ EELAALQARW EQEKALAAQI GEARASVEAA SAQQDGGTAS QAHDIQALLK
ELRALQGEAP MVPVQVDGNV VAEIVAGWTG IPLGKMVKDE IQAVLKLRPA LEERVIGQPH
ALEAVAQRVR TARANLDDPN KPKGVFLFVG PSGIGKTETA LALADALYGG ERKMVTINMS
EYQEAHSVSG LKGSPPGYVG YGEGGVLTEA VRRNPYSVVL LDEVEKAHPD VLELFFQVFD
KGVMDDAEGR EIDFRNTIII LTSNVGSATM MQACLNKEAE EMPAPEELEA AIRPQLVKAF
KPAFLGRLKV VPYYPLGDDV LASIITLKLD RIGQRVAANH KATFHYDDTL VEAVLARCTE
VDSGARNVDN ILNGTLLPEV AEAVLAKMAE GSAIGRIEVA ADQQGNFSYS VA
//
