GenomeNet

Database: UniProt
Entry: A0A494XTV9_9BURK
LinkDB: A0A494XTV9_9BURK
Original site: A0A494XTV9_9BURK 
ID   A0A494XTV9_9BURK        Unreviewed;       885 AA.
AC   A0A494XTV9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:RKP50973.1};
GN   Name=tssH {ECO:0000313|EMBL:RKP50973.1};
GN   ORFNames=D7S89_07920 {ECO:0000313|EMBL:RKP50973.1};
OS   Trinickia fusca.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP50973.1, ECO:0000313|Proteomes:UP000280434};
RN   [1] {ECO:0000313|EMBL:RKP50973.1, ECO:0000313|Proteomes:UP000280434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP50973.1,
RC   ECO:0000313|Proteomes:UP000280434};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL   Submitted (OCT-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}.
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:RKP50973.1}.
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; RBZV01000002; RKP50973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494XTV9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000280434; 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; 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:UP000280434};
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   REGION          170..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  96003 MW;  2BCF1D0193B90EDE CRC64;
     MSTPLKTLIA KLDALCLDAA TRAASLCLAR GHYEVDLEHL FLTLLEDKTS DLCVVLRTNK
     LSVDMLRSDL ERELEGLKTG NTRTPVFSPH LIALFEQAWL IASLDSQAAR IRSGHLLLAL
     LVAPDLAQFA QRMSSVFSRI AVEHLKHKFD ETTAGSSEAM RAVEAGEGAG ALDAASDPIP
     QPGASKTPAL DTYTTNLTQR AREGNIDPVI GREAEIRQTI DILMRRRQNN PILTGEAGVG
     KTAVVEGLAL RIAAGDVPGP LVGVALHVLD MGLLQAGASV KGEFENRLKN VIDEVKKSAV
     PIVLFIDEAH TIIGAGGQAG QNDAANLLKP ALARGELRTI AATTWSEYRK YFEKDVALAR
     RFQVVKIEEP NEMLAAAMVR GLAARMEAHF KVRILDEAIT EAVRLSHRYI TGRQLPDKAI
     GVLDTACAKV ALAHGSTPAA IDDARKRIER IDVEIASLER ETATGMTGAA HEERLAELRR
     ARDTDVTGLA LDEARYEQER ALVTRIGTLR CELEAASPDQ AGTARAALAQ ATGELQALQQ
     AHPMVPLQVD AHVVAQIVAS WTGIPLGSMV KDEIDTVLNL QDLLTARVIG QDHALDAIAQ
     RVRTASANLE DPNKPRGVFL FVGPSGVGKT ETALALADIL YGGERKLVTI NMSEYQEAHS
     VSGLKGSPPG YVGYGEGGVL TEAVRRNPYS VVLLDEVEKA HPDVLEMFFQ VFDKGTLDDA
     EGREIDFRHA LIILTSNVGS SNVMQACLNK PAEELPSADE LAETLRPQLY KAFKPAFLGR
     LKVVPYYPIS DDVLAEIIEL KLSRIRDRIA ANHRAVFAWD ESLVDAVLAR CTEVDSGARN
     VDHILNGTLL PELAQHVLGR IAQGERIERI EARALESGQF EYKVA
//
DBGET integrated database retrieval system