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}.
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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
//