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
//