ID   A0A126ZFH6_9BURK        Unreviewed;       892 AA.
AC   A0A126ZFH6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:AMM25716.1};
GN   ORFNames=AX767_16135 {ECO:0000313|EMBL:AMM25716.1};
OS   Variovorax sp. PAMC 28711.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM25716.1, ECO:0000313|Proteomes:UP000070169};
RN   [1] {ECO:0000313|EMBL:AMM25716.1, ECO:0000313|Proteomes:UP000070169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM25716.1,
RC   ECO:0000313|Proteomes:UP000070169};
RA   Park H.;
RT   "Complete genome of Variovorax sp.";
RL   Submitted (FEB-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; CP014517; AMM25716.1; -; Genomic_DNA.
DR   RefSeq; WP_068632259.1; NZ_CP014517.1.
DR   AlphaFoldDB; A0A126ZFH6; -.
DR   STRING; 1795631.AX767_16135; -.
DR   KEGG; vaa:AX767_16135; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000070169; 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; 2.
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:UP000070169};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          9..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          437..488
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   892 AA;  96309 MW;  18E53239D5C7911B CRC64;
     MSTSLKTLIT KLNPTARSAT ERAANLCLSR GHYEVDLEHL FLALLEQPGN DIARVLRANK
     VSPTALQSDL EREIAAFKNG NARTPVFSQY LQKLFQHAWL LASLDAHVTA IRSGHLLLAL
     LTEPDLAQLA QRGSPLFAKI RLEDLKHDFD KVTDGSDEAI DAGAARTDDR AVSSDAVAVP
     GKTPALDQFT TNLTQRARDG SLDPVIGRDT EIRQVIDILM RRRQNNPILT GEAGVGKTAV
     VEGLALRIAV SDVPDVLKGV EVHTLDMGLL QAGASVKGEF ENRLKNVIAE VKKSAHPIVL
     FIDEAHTMIG AGGAAGQNDA ANLLKPALAR GELRTIAATT WGEYKKYFEK DAALARRFQV
     VKVEEPTEVL AAAMLRGMVP LMEKHFNIRV LDEAITEAVR LSHRYITGRQ LPDKAVGVLD
     TACARVALGQ SATPALIEEA RKAIERLDAE TAALDRDTAA GGAHSARLAE LVEQKAAAQA
     SLVEKEARLV KESALVLRIH ALRAERDAAT SAVLAEPPVA RKKGAARSPG RVDELGELLG
     ELRALQGDAP MMPLQVDGHV VAEIVSAWTG IPLGRMVKDE IRTVRNLEAL LAERVIGQDH
     ALAAVAQRVR TASARLEDPN KPRGVFMFVG PSGVGKTETA LALADILYGG EKKLITINMS
     EYQEAHSVSG LKGSPPGYVG YGEGGVLTEA VRRQPYSVVL LDEVEKAHPD VMEMFFQVFD
     KGLMDDAEGR EIDFRNTLII LTSNVGSSQI MQACLNKTSA ELPAPDALAE ALRPALMKSF
     KSAFLGRLKV APFYPITDDV LAQIIELKLG RIRDRIAPNH KAVFDWDASL VDSVLARCTE
     VDSGARNVDH ILNGTLLPEI AGAVLARMAD EAAITKIKVS SGKNGDFKYK IS
//