ID A0A1I4WQL8_9NEIS Unreviewed; 881 AA.
AC A0A1I4WQL8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Type VI secretion system protein VasG {ECO:0000313|EMBL:SFN16068.1};
GN ORFNames=SAMN05660284_00686 {ECO:0000313|EMBL:SFN16068.1};
OS Formivibrio citricus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Formivibrio.
OX NCBI_TaxID=83765 {ECO:0000313|EMBL:SFN16068.1, ECO:0000313|Proteomes:UP000242869};
RN [1] {ECO:0000313|Proteomes:UP000242869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6150 {ECO:0000313|Proteomes:UP000242869};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOVE01000004; SFN16068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4WQL8; -.
DR STRING; 83765.SAMN05660284_00686; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000242869; 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: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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000242869};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 226..371
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 608..765
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 786..878
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 160..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 95616 MW; AAF4E418413FE15C CRC64;
MTIPLKALVD RLTPPARRAF EDAASRALAR THFEVEIEHV LLAVLAQDSN AALSTLHTLD
MNPSPVERGL EAALDGFRCG NTRNPVLSSW LPKWLEKAWL SASAEFGQED ISTLDLLVAL
LRDASLRNTL QASMPMLGTM DVEKAVSAYS TLRRHGGEAL GSADADQARS AALQPEPDAP
SCRRGSPALD KYTIDLTAQA RAGKIDPVLG RDVEIRQMID ILQRRRQNNP ILTGEPGVGK
TAVVEGLARK IVAGEVPPVL IGVTLRTLDL GLLQAGASVK GEFENRLRQV IDEVKASTTP
IILFIDEAHT LIGAGGAAGQ NDAANLLKPA LARGELRTIA ATTWAEYKKY FEKDAALARR
FQVVKVDEPA PEVAVQMVRG IAQAMAKHHG VEILNEAVVS AVHLSSRYIT GRQLPDKAIS
VLDTACARVA LSRAGRPAPI EDIEVLLANI DREIAALQQE GGHAERIGEL QAQRTALETD
LQAHHSAWEQ QKLLVAEIDE LKTNPAKHAA KPGRGKKLSA LQARRNALKD LQKHQPLAFE
CVDENVIADV ISGWTGIPLG RMVSNELEQV RQLADLLAQR VIGQDHALRQ IAERIKIAKA
NLDDPSKPKG IFLLVGPSGV GKTETALALA EALYGGERNL ITINMSEYQE AHSVSGLKGS
PPGYVGYGEG GVLTEAVRRK PYSVVLLDEV EKAHPDVLEL FFQVFDKGML EDGEGREVDF
KNTIIQLTSN AGSEIVMRAL EHGVQAGDET RSPTPDDLVE LLRPTLQQVF SPAFLGRLDI
VPYFPISDDV LRRIVSLKLE KIRRRIAENH GAHVEFPEEL VDLVVARCLD VDSGARDAEA
ILTRTVLARI SSDLLGHMAS GKPVKKIAVS LKGDDLKVKL S
//
