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Database: UniProt
Entry: A0A4R5MFQ7_9BURK
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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
//
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