ID A0A0S9MSZ0_9BURK Unreviewed; 886 AA.
AC A0A0S9MSZ0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=ClpV1 family T6SS ATPase {ECO:0000313|EMBL:KQP35436.1};
GN ORFNames=ASF44_19015 {ECO:0000313|EMBL:KQP35436.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP35436.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP35436.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP35436.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP35436.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP35436.1,
RC ECO:0000313|Proteomes:UP000051759};
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:KQP35436.1}.
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DR EMBL; LMNA01000030; KQP35436.1; -; Genomic_DNA.
DR RefSeq; WP_056902595.1; NZ_LMNA01000030.1.
DR AlphaFoldDB; A0A0S9MSZ0; -.
DR STRING; 1736318.ASF44_19015; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051759; 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..156
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
SQ SEQUENCE 886 AA; 96777 MW; 67C37C335542BA6E CRC64;
MSEISRVALF GKLNPLAYKA IESATVFCKM RGNPYVELVH WFVQLVQNNE TDLDAILRHY
QVDASAMARD MTAALDRLPR GSTAISDFSE QIENAIERAW VYATLQFGEA QVRTGTLVIG
MMKSTHLRNA LLAISKEFAK VRADDLADNF AKICGGTAES KLGAQDGTGI GSGEPGGDSG
AMAPAAMGKG EALKKFCVDM TERAREGKMD PVTGRDEEIR QIVDILMRRR QNNPILTGEA
GVGKTAVVEG FAQRLARGDV PPQLQEVSLL SLDLGLLQAG ASMKGEFEQR LRQVIDEVQA
SPKPIILFID EVHTLVGAGG AAGTGDAANL LKPALARGNL RTIGATTWAE YKKYIEKDPA
LTRRFQVVQV PEPDEAKAVL MLRGVATVLE KHHRAQLLDE AIEAAVRLSH RYIPARQLPD
KAVSLLDTAC ARVAVSQHAT PAEVEDCTRR IEALEIEEGI IARELAVGVQ VGTRGTEVAE
KLASERERLV GLQAKWKDEK AVVDQVLALR ARLRLEGEEA KSVDREAVLS ELRGAQEKLA
ALQGESPLIM PSVDAQAVAS VVSDWTGIPV GRMVKNELEN ILRLGETLGQ RVIGQQHGLD
MIAKRIQTSR ARLDNPNKPI GVFMLCGTSG VGKTETALAL AEALYGGEQN VITINMSEFQ
EAHTVSTLKG SPPGYIGYGE GGILTEAVRR RPYSVVLLDE VEKAHPDVHE LFFQVFDKGR
MEDGEGRMID FKNTIILLTS NAGSELVMNM CKDPELLPDP ESLATALQEP LMKIFPPALL
GRLVTIPYYP LSPEMMGKII RLQLNRIKKR VEANHKIPFH YEQEAVDLIV KRCDNPEAGG
RIIDSILTNT VLPKISVEYL SRMSQGQELQ GITLGASGGE FTYRFD
//