ID A0A2U8FTH2_9BURK Unreviewed; 927 AA.
AC A0A2U8FTH2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:AWI54187.1};
GN Name=clpV {ECO:0000313|EMBL:AWI54187.1};
GN ORFNames=DEH84_12725 {ECO:0000313|EMBL:AWI54187.1};
OS Aquabacterium olei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1296669 {ECO:0000313|EMBL:AWI54187.1, ECO:0000313|Proteomes:UP000244892};
RN [1] {ECO:0000313|EMBL:AWI54187.1, ECO:0000313|Proteomes:UP000244892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110486 {ECO:0000313|EMBL:AWI54187.1,
RC ECO:0000313|Proteomes:UP000244892};
RA Tang B., Chang J., Zhang L., Yang H.;
RT "complete genome sequence of Aquabacterium olei NBRC 110486.";
RL Submitted (MAY-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}.
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DR EMBL; CP029210; AWI54187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8FTH2; -.
DR KEGG; aon:DEH84_12725; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000244892; Chromosome.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000244892};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 9..155
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 153..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..493
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 927 AA; 99998 MW; FF8351F62DD0893D CRC64;
MSQNLKTLIS KLNDATRQAA ERAASLCMGR GHYEVDIEHL LLALLEQPGN DLSVLAQRAN
VSLTELQRDI EAELAGFKTG NTRTPVFSAH LPVLLEHAWL IASLESAVAR IRSAHLLLAL
LTEPTLSQLA HRTSRLFARF SLEDLKHRLA EVTRGSTEAV TPAAAGSVQD DGGDGDEADA
ADALSGKTPA LDQFTTNLTE RAREGKVDPV IGRDAEIRQA IDILMRRRQN NPILTGEAGV
GKTAVVEGLA LRVAQGDVPP PLQGVAIHVL DMGLLQAGAS VKGEFENRLK NVIDEVKRST
HPIILFIDEA HTMIGAGGQA GQNDAANLLK PALARGELRT IAATTWGEYK KYFEKDAALA
RRFQVIKVEE PSEELACAML RGMAPLMEKH FGVRLLDDAI REAVRLSARY ISGRQLPDKA
VSVLDTACAK VALGQSATPA RIEEARKRLE RLDAEAAALL REAAIGARHG ERLDALKAER
NAIVQQLQAD ETRWSHEQQL VSDIQALRAK LEQQAGGLSS AEAGLATTTA DTAAPEGTSK
AAKSRKKMDA SPASPDHELL AGKQAELGAL QGEAPLVPMQ VDGHVVAEIV AAWTGIPLGK
MVKDEIRTVR NLQGTLQERV IGQDHALAAI AQRVRTARAG LEDPNKPKGV FLFVGPSGVG
KTETALALAD ILYGGERNLI TINMSEYQEA HSVSGLKGSP PGYVGYGEGG VLTEAVRRKP
YSVVLLDEVE KAHPDVLEMF FQVFDKGVMD DAEGREIDFR NTVIILTSNA GSQQIMNACF
RQDEELGGPV MRSVDEMPAA DELAEALRPV LYKTFKPAFI GRTKVVPYYP LNDDVLVDVI
KLKLDRIAAR VAANHQAELS YDDALVESVL ARCTEVDTGA RAVDHILNGS LLPEVAESVL
ARMAEGQPIQ RIKVSAAKDG AFRFKVA
//