ID A0A2G8TB24_9BURK Unreviewed; 877 AA.
AC A0A2G8TB24;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:PIL43245.1};
GN Name=clpV {ECO:0000313|EMBL:PIL43245.1};
GN ORFNames=CR105_19710 {ECO:0000313|EMBL:PIL43245.1};
OS Massilia eurypsychrophila.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1485217 {ECO:0000313|EMBL:PIL43245.1, ECO:0000313|Proteomes:UP000230390};
RN [1] {ECO:0000313|EMBL:PIL43245.1, ECO:0000313|Proteomes:UP000230390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30074 {ECO:0000313|EMBL:PIL43245.1,
RC ECO:0000313|Proteomes:UP000230390};
RA Wang H.;
RT "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL Submitted (OCT-2017) 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:PIL43245.1}.
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DR EMBL; PDOC01000015; PIL43245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8TB24; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000230390; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000230390};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..156
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 157..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 94856 MW; 3715FDB7FB2D81C9 CRC64;
MDINLKTLIG KLNDCSRAAA SRAAGICVSQ GHYEVDIEHL FLALLEQPNC DFACIARQCG
ISATGIETDL RNEISRFAKG SARTPVFSRH LPTLLEHAWL IASLGGGGPH QIRSGHLLLA
LLTAPDLAQL AQRGSKLFAQ VPIDRLKHDF DKLTRSSDEA VLSAPSESGG GDPVSDLEHG
GAHKTPALDQ FTTCLTQRAR DGKLDPVIGR DPEIRQAIDI LMRRRQNNPI LTGEAGVGKT
AVVEGLALRI ASGDVPEVLC GVEIHTLDMG LLQAGASVKG EFENRLKNVI DEVKKSPHAI
ILFIDEAHTM IGAGGAAGQN DAANLLKPAL ARGELRTIAA TTWGEYKKYF EKDAALARRF
QVVKVEEPDE ATACAMLRAM APLMEKHFGV RVYDDAIEEA VRLSHRYISG RQLPDKAISV
LDTACAKVAL GQSATPALVE AGGRLLERID AQVAALTREE SAGADHAAKL TALRAERRAA
VEAQRDVQKR WQQEQAINSE IQALRSSMEQ GGGDGARLRG LIEQLRTVQG EAPLVPVQVD
GHVVAEIVAG WTGIPLGRMV KDEIRMVMNL QGLLEERILG QSHAGAVVAQ RVRTARANLD
DPNKPKGVFL FVGTSGVGKT ETALALADLL YGGERKLITI NMSEYQEAHS VSGLKGSPPG
YVGYGEGGVL TEAVRRNPYS VVLLDEVEKA HPDVLELFFQ VFDKGVLDDA EGRQIDFRNT
IIILTSNAAS SQMMQACLNK SASEMPDPTQ LAAIIRPQLM KHFKPAFLGR LTVVPFYPIG
DEVLGRIIRL KLERIRRRID QNHQAQFDYD DALVNAVLSR CTEVDSGARN VDTILNGTLL
PEIADSVLAR MAEGGAIARI KVSATKAGKF KYAVEPC
//
