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Database: UniProt
Entry: A0A4R5M4N1_9BURK
LinkDB: A0A4R5M4N1_9BURK
Original site: A0A4R5M4N1_9BURK 
ID   A0A4R5M4N1_9BURK        Unreviewed;       925 AA.
AC   A0A4R5M4N1;
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:TDG20342.1};
GN   Name=tssH {ECO:0000313|EMBL:TDG20342.1};
GN   ORFNames=EYW47_26190 {ECO:0000313|EMBL:TDG20342.1};
OS   Paraburkholderia silviterrae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2528715 {ECO:0000313|EMBL:TDG20342.1, ECO:0000313|Proteomes:UP000295722};
RN   [1] {ECO:0000313|EMBL:TDG20342.1, ECO:0000313|Proteomes:UP000295722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4M-K11 {ECO:0000313|EMBL:TDG20342.1,
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}.
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:TDG20342.1}.
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DR   EMBL; SMRP01000016; TDG20342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R5M4N1; -.
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; 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:SF181; ATPASE SUBUNIT OF ATP-DEPENDENT PROTEASE-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.
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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          18..158
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          903..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  99834 MW;  701D5B83337A8B6D CRC64;
     MPMRDDRRKS LRDTSQLLRQ LNPHCASALE AAASLCQTRL ADEITVEHWL LKLIEAGDGD
     IPAIVRHYDI DIDAVWDALI GAIDHLPRSL RGRPALSPQL ATVLQDASLH ASAEADEIVI
     RSAHVLQAIV DAPHVLRARN AWPLLSMSSA QIRRLLPRLG NRTCEAPVEE PPAPTTQSTP
     TLAATETTGM TGATATTNSL PPSTPHKVEG DALARFAIDI TQKARDGKID PVFGRDREIQ
     QMVDVLARRR KNNPILVGEP GVGKTALVEG LALRVAEGTV PNVIREVRIL TLDLGLLQAG
     AGVKGEFEQR LKNVIDEVQT SAVPILLFID EAHTMIGAGN AAGGADAANL LKPALARGEL
     RTIAATTWSE YKQYFERDAA LERRFQVIKV EEPDDDAACL MLRGLKERYA RYHNVHIRDE
     ALVAAVRLSR RYIPARQLPD KAVDLIDTAA ARVRMGLESP PAELQRARAR VATLELEGAT
     LDADRQAGIE PSSARQEALE TALAGAQVEL AALHARYEVE LERVHAIETL RTADPSARDA
     AAFVHARQAL ANAQGKAPLI FADVNADAVA RVVAEWTGVP VGSLVEDELL GLLALEARLS
     TRVVAQDDAL AALAESLRTA KAGLKNEHAP LGVFLLAGPS GVGKTETALA LADVLFGGEA
     ALTTINMSEY QESHTVSQLK GSPPGYVGYG RGGILTEAVR QRPYSVILLD EVEKAHRDVL
     DLFYQVFDRG TMRDGEGREI DFRNCVILMT SNLGSEQIDE ASGDNPAVSH AQLLDAIRPQ
     LLAHFQPALL ARFQTLVYRP LDAAALAAIV RLKLAKVAQR LHRQHDVAFV CDDSLIDAIA
     ELCLERHSGA RNVDAFLNQH VLPTVSRELL ARMASGALPA QIRLASSPEG NLTIDFVDAP
     EGHADEVDAD EAESTQAADP VRAGA
//
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