ID A0A523Q310_9BURK Unreviewed; 920 AA.
AC A0A523Q310;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=Type VI secretion system ATPase TssH {ECO:0000313|EMBL:TDM05867.1};
GN Name=clpV {ECO:0000313|EMBL:TDM05867.1};
GN ORFNames=C4K60_14315 {ECO:0000313|EMBL:TDM05867.1};
OS Ideonella sp. MAG2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Ideonella.
OX NCBI_TaxID=2083017 {ECO:0000313|EMBL:TDM05867.1, ECO:0000313|Proteomes:UP000319140};
RN [1] {ECO:0000313|EMBL:TDM05867.1, ECO:0000313|Proteomes:UP000319140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAG2 {ECO:0000313|EMBL:TDM05867.1};
RA Richards S., Han Y., Dugan S., Qu J., Doddapaneni H., Dinh H., Chao H.,
RA Hughes D., Muzny D., Lee S., Murali S., Worley K., Gibbs R., Poynton H.,
RA Poelchau M., Werren J., Bowen J., Vineis J.;
RT "Bacterial draft genomes recovered from genome assembly of Hyalella
RT azteca.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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:TDM05867.1}.
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DR EMBL; PTEU01000002; TDM05867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A523Q310; -.
DR Proteomes; UP000319140; 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; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
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; 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.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000319140}.
FT DOMAIN 227..372
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 618..761
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 790..881
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 158..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 99541 MW; 0C356C4C0656D19A CRC64;
MQTVRRSLFS KLSTRLFQQL ESATALASER GDPEVSLGHW LLQIWHLESA DLRLICAHFE
LDDTEVLQGF SASLGRRGLR LDRKGLDFSP DIELAIERAW LLASVQANDH KIRSAWLLMA
LLQTPALCKA LYAISSEFQR LPKSGLFAQV QHLLSDSLES EDSAQSGGGK PASPEASGGP
AAAPGSDSAL STYCTDLTQW AREGKIDPVV GRDREIRVLM DVLLRRKQNN PLLVGEAGVG
KTAVVEGLAH AIARAQVPTP LKGVRLLSLD IGGLLAGAAM RGEFEARLRS VLDESTQSSQ
PTILFVDEVH TLVGAGGSAG TGDAANLLKP ALARGQLRLI GATTWSEYKR HIEKDPALTR
RFQAQLIEEP DDARAFMMVR SLVGPFQRHH GVHIRDEAVA SAVTLSRRYL PARQLPDKAI
SLLDTACARV ALTQHVPPAL LQAKQQALAD LERQRNAAQQ DAQLRPGPHP QVQQLQQQLE
AAQAELSTLN QRWEALQALL QAWGAARDAL QTHPDPAADA PVAQEQAQQD MARLSADIER
SPLWSAQQSL VVDHEAVAAV VSEWTGVPAG QMLKDDVRAM AQLQARLETR VLGQSWALRT
IADRIKAARA QLTDPGKPLG VFMLVGPSGV GKTETALALA EAVYGGAQNL ITINMSEYQE
AHTVSSLKGS PPGYVGFGEG GVLTEAVRRR PYSVVLLDEV EKAHPDVHEI FYQVFDKGWM
DDGEGRTIDF TNTLILLTSN VGAELIQECC ADEAVKPGAA QLVSLLDAPL RAVFPAAFLG
RVSVVPYLPL DPSRLSAIAR LQLAKVEARM RTAHGLGFNA SDAAVQSLIA QCGINDTGAR
RISQFIEQHI LPAIAQRWLD AQEHGASLTT LSLEWMPETQ VDAIDPAGHL VLRSDATPHP
ASGQLQFPGP FSTLTDQETP
//