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Database: UniProt
Entry: A0A370NA14_9BURK
LinkDB: A0A370NA14_9BURK
Original site: A0A370NA14_9BURK 
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}.
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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
//
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