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
//