ID A0A370NA14_9BURK Unreviewed; 890 AA.
AC A0A370NA14;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:RDK02450.1};
GN Name=clpV {ECO:0000313|EMBL:RDK02450.1};
GN ORFNames=DLM46_12720 {ECO:0000313|EMBL:RDK02450.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDK02450.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) 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, ECO:0000256|RuleBase:RU004432}.
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:RDK02450.1}.
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; QHKS01000007; RDK02450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370NA14; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000254875; 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; IPR028299; ClpA/B_CS2.
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.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000254875};
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 890 AA; 96909 MW; 3869197251276E0B CRC64;
MAEISRVALF GKLNGLAYRA IESSTVFCKL RGNPYVELSH WIHQILQLQD SDLHRIIRHF
DLDAAVLARD LTAALDRMPR GSTSVTDLSS QVEEAVERAW VYGTLMFGES QVRTGYIMVG
LLKTPGLRHS LHAISRQFEK VKSETLADAF NEIAGGSPEA NLPATDNFQM GAAAPGEASG
ALAPAALGKG EALKRFTLDL TEQARSGKLD PIVGRDEEIR QVIDILMRRR QNNPILTGEA
GVGKTAVVEG FAQRIVAGDV PPQLRDVRLL TLDVGLLQAG ASMKGEFENR LRQVIEEVQA
SEKPVILFID EAHTLVGAGG AAGTGDAANL LKPALARGTL RTVAATTWAE YKKHIEKDPA
LTRRFQVVQV PEPSEDKALL MMRGIASSLE THHRVQILDE ALDAAVKLSH RYIPARQLPD
KAVSLLDTTC ARVAVSQHAT PAAIDDARKR IAALETELAI IGRETAVGVD TLERETLATQ
KLVAERARLA ELDARWQTEK TLVDRILELR GKLRDATGKV EGAADTGSAE TWLAQLKDLQ
AQLAAHQGET PLILPTVDHQ AVASVVQDWT GIPVGRMVKN EIENVLKLAD TLSQRIIGQR
HALDMIARRI QTSRAGLDNP GKPIGVFMLA GTSGVGKTET ALALAEALYG GEQNVITINM
SEYQEAHTVS SLKGAPPGYV GYGEGGVLTE AVRRRPYSIV LLDEVEKAHP DVHEIFFQVF
DKGWMEDGEG RVIDFKNTLI LLTTNAGTDL ITSLCKDPDL MPDADGIAKA LREPLLKVFP
PALLGRLVTI PYYPLNDEMI GAIIRLQLGR IARRVAQSHK VPFTYDDEVV RLIASRCTEL
ESGGRMIDAI LTNSLLPAIS GEFLTRLMDG KPVRRAHITV SNGEFGYAFD
//