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Database: UniProt
Entry: A0A2S4MK98_9BURK
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Original site: A0A2S4MK98_9BURK 
ID   A0A2S4MK98_9BURK        Unreviewed;       912 AA.
AC   A0A2S4MK98;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Type VI secretion system protein VasG {ECO:0000313|EMBL:POR55055.1};
GN   ORFNames=B0G62_102666 {ECO:0000313|EMBL:POR55055.1};
OS   Paraburkholderia eburnea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR55055.1, ECO:0000313|Proteomes:UP000237381};
RN   [1] {ECO:0000313|EMBL:POR55055.1, ECO:0000313|Proteomes:UP000237381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18070 {ECO:0000313|EMBL:POR55055.1,
RC   ECO:0000313|Proteomes:UP000237381};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JAN-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:POR55055.1}.
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DR   EMBL; PQGA01000002; POR55055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4MK98; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000237381; 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; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237381};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          18..166
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          461..527
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   912 AA;  98371 MW;  4C4E281E7C59F2A0 CRC64;
     MTVHHDRNAY LRDASQLLQR LNPHCANALE AAASLCQTRL ADEITVEHWL LKLIEAGDGD
     IPAIMNHYEL NIDAVWDALL RAIDHTPRNL RGRPSLSPQL AAVLQDAWSH ALNLADSGET
     AIRSANVLQA IVEAPHVLRA ANAWQLLSVS TAQIERLLPR LGLRTCENQP EEPEAPADPT
     VAPTQAGAVN EAAEGKPAPA ARRSVEGDAL ARFAIDITAK AREGKIDPVF GRDREIQQMV
     DVLARRRKNN PILVGEPGVG KTALVEGLAL RVAEGTVPNV IRDVRILTLD LGLLQAGAGV
     KGEFEQRLKN VIDEVQASDV PILLFIDEAH TLIGAGNAAG GADAANLLKP ALARGELRTI
     AATTWSEYKE YFERDAALER RFQMIKVEEP DDSAACLMLR GLKERYATYH NVHIRDEALV
     AAVRLSRRYI PARQLPDKAV DLIDTAAARV RMGLESPPAE LQRARAAVAA LELELVTLED
     DARAGVEVAE ERRASLHDAL ANAKDQLETL QQRYGRELNL VQSLLEQRGA TTGTAELAQT
     RDALAQAQGK APLIFADVDA QAIARVVAEW TGVPVGNLLE DELQGLLTLE EQLAKRVVAQ
     DEALGALAES LRTAKAGLKN EHAPLGVFLL AGPSGVGKTE TGLALADLLF GGEAALTTIN
     MSEYQESHTV SQLKGSPPGY VGYGRGGVLT EAVRQRPYSV VLLDEVEKAH RDVLDIFYQV
     FDRGTMRDGE GREIDFRNCV ILMTSNLGSA QIDEVTTDNP EIAQAALLEA IHPQLVAHFQ
     PALLARFQTL AYRPLDVGAL AAIVRLKLAK VAERLRRQHG VELVCADSLI GSMAELCLAR
     ESGARNVDAF LNQRILPSVS RELLTRMASG TAPAKILLSS SAEGNLTIDF LDHGEPAAAP
     AATTAEPAAL AT
//
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