ID A0A4R5MFQ7_9BURK Unreviewed; 914 AA.
AC A0A4R5MFQ7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:TDG26119.1};
GN Name=tssH {ECO:0000313|EMBL:TDG26119.1};
GN ORFNames=EYW47_01810 {ECO:0000313|EMBL:TDG26119.1};
OS Paraburkholderia silviterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2528715 {ECO:0000313|EMBL:TDG26119.1, ECO:0000313|Proteomes:UP000295722};
RN [1] {ECO:0000313|EMBL:TDG26119.1, ECO:0000313|Proteomes:UP000295722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4M-K11 {ECO:0000313|EMBL:TDG26119.1,
RC ECO:0000313|Proteomes:UP000295722};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. 4M-K11, isolated from subtropical forest soil.";
RL Submitted (MAR-2019) 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:TDG26119.1}.
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DR EMBL; SMRP01000001; TDG26119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R5MFQ7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000295722; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 524..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 445..496
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 914 AA; 99878 MW; A18ABCDD2B8310E4 CRC64;
MAEIKRAALF GKLNQLGFRA LESANMFCRL RGNPYIELVH WFHQILQLQD SDLHRLVRHY
GIDPARLAGD LTAALDRLPR GASSVTDISS QVEEAVERGW VFGSLMFGES QVRTGHLIVG
LLKTPSLRNT LYGISRQFES IKLDALCEEF DRLLRDSPEA AMAASDGFKA NAGTGAEGDA
TGMPPAAMGK QEALRRFTTD LTEQARSGKL DPIVGRDEEI RQVVDILMRR RQNNPILTGE
AGVGKTAVVE GFAQRIVAGD VPPSLRDVEL RTLDVGLLQA GASMKGEFEN RLRQVIEEVQ
ASEKPVILFI DEAHTLVGAG GAAGTGDAAN LLKPALARGT LRTVAATTWA EYKKHIEKDP
ALTRRFQVVQ VGEPDEEKAI RMMRGVASTM EQHHKVQVLD EALEAAVRLS HRYIPARQLP
DKSVSLLDTA CARVAVSQHA TPPSVDDARK RIASLETEME IIGREKAVGI ETREREASAS
EKLAVERERL AQLEARWETE KGLVERILAL RAQLRERTGK VEGGALASGE GAAPAGNDTN
AANGANGAAP VDAEALRAEL RELQAQLASH QGEEPLILPT VDRQAVASVV QDWTGIPVGR
MVRNEIENVL KLAENLNKRI IGQGHATEMI ARRIQTSRAG LDNPNKPIGV FMLAGTSGVG
KTETALALAE VLYGGEQNVI TINMSEYQEA HTVSSLKGAP PGYVGYGEGG VLTEAVRRRP
YSVVLLDEVE KAHPDVHEIF FQVFDKGWME DGEGRVIDFK NTLILLTTNA GTDLITNLCK
DPELMPDPEG IAKALREPLL KVFPPALLGR VVTIPYYPLS DEMLGAIIRL QLSRIEKRLR
VSHKVPFLYD DEVVKLIASR CTELESGGRM IDAILTNTLL PRVSTEFLTR MMNGGSVTKV
QVGARDGEFV YTFD
//