ID A0A0C1Y6F0_9BURK Unreviewed; 896 AA.
AC A0A0C1Y6F0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=ATPase AAA {ECO:0000313|EMBL:KIF82523.1};
GN ORFNames=TSA66_19630 {ECO:0000313|EMBL:KIF82523.1};
OS Noviherbaspirillum autotrophicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF82523.1, ECO:0000313|Proteomes:UP000031572};
RN [1] {ECO:0000313|EMBL:KIF82523.1, ECO:0000313|Proteomes:UP000031572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA66 {ECO:0000313|EMBL:KIF82523.1,
RC ECO:0000313|Proteomes:UP000031572};
RA Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL Submitted (DEC-2014) 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:KIF82523.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JWJG01000028; KIF82523.1; -; Genomic_DNA.
DR RefSeq; WP_040041197.1; NZ_JWJG01000028.1.
DR AlphaFoldDB; A0A0C1Y6F0; -.
DR STRING; 709839.TSA66_19630; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000031572; 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; 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:UP000031572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..155
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 470..514
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 896 AA; 97798 MW; A8ED22C2D8A3B266 CRC64;
MTTNLKMLIA KLNPICTKAA EQAVNDCVSR GHYEVDLEHL FLALLSDAQS DVTLLLKHYG
INAQALENDL LDELAALRGG NSRTPVFSAH LLRLFEHAWL LASLDGEAMR IRSAHLLLAL
LAQPDLSQLA YRASQQFMRF SAADIKHKLS ELTAGFPETP CIANGAVDTT GSDASEDSAA
RTGKTPALDQ FTANLTQRAK DGKIDPVIGR DAEIRQVIDI LMRRRQNNPI LTGEAGVGKT
AVAEGLAQRI AEGDVPPALT GVALHVLDLG LLQAGASVKG EFENRLRNVI EEVTRSPHPI
ILFIDEAHTM IGAGGQAGQN DAANLLKPAL ARGELRTIAA TTWSEYKKYF EKDAALARRF
QVVKVGEPSE AVACAMLRGL AARMESHFGV RVMDDAIVDA VRLSARYISG RQLPDKAISV
LDTACARVAT GQSAIPAAIE DARRLDDLLS VEISSLEREL SAGAPHLERL AELRDRRDTN
RSILKAHEER WEKERQLAKQ IQALRARLES AQGEVGECMA SRSGRKGGAT AAKPEMKALA
SLREELRALQ GETPLVPVCV EAQTVGEIVA AWTGIPLGRM VKDEIKTVLN LKPLLEQRVV
GQSHALEQIA QRVRTARAHI EDPNRPKGVF LFVGPSGVGK TETALALADI LYGGERNLVT
VNMSEYQEAH SVAGLKGSPP GYVGYGEGGV LTEAVRRKPY SVVLLDEVEK AHPDVLELFF
QVFDKGVMDD AEGREIDFRN TVIILTSNVA SQSIMQACLN KAADELPDME NLGEMIRPQL
YKAFKPAFLG RMKVIPYFPL PDEILADIIR LKLDRIRHRI ETNHKAAFSY SEEVVDAVLA
RCTEVDAGAR NVDHILNGTM LPQIAETVLG RMAEGKTIKN VRVAVGKRSE FSYKIN
//
