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Database: UniProt
Entry: A0A523Q310_9BURK
LinkDB: A0A523Q310_9BURK
Original site: A0A523Q310_9BURK 
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
//
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