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
//