ID V9EP52_PHYPR Unreviewed; 685 AA.
AC V9EP52;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpX {ECO:0000313|EMBL:ETI40278.1};
GN ORFNames=F443_14292 {ECO:0000313|EMBL:ETI40278.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI40278.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI40278.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI40278.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:ETI40278.1}.
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DR EMBL; ANIZ01002472; ETI40278.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EP52; -.
DR EnsemblProtists; ETI40278; ETI40278; F443_14292.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_6_0_1; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00382; clpX; 1.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:ETI40278.1};
KW Hydrolase {ECO:0000313|EMBL:ETI40278.1};
KW Nucleotide-binding {ECO:0000313|EMBL:ETI40278.1};
KW Protease {ECO:0000313|EMBL:ETI40278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 359..510
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 566..660
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 152..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 74376 MW; 2C8E97BA1726DBCF CRC64;
MLRRLRPDTS ALACVSHLLQ PTHMSAVPSP CRTFSQLSTT PHRLQRLPTA YATRGVVTGP
PSDSHKKKAA GDQLCCPQCG AALVLAEPLG SADKSTSSTS TSTSPVEFKK GDVVKCVTCN
LHFALKAQPP AQPSPTFRNA AAAAALSSLS SSLSPSMQTT RGSSLGGPTY SGNFPSSTRG
GRMNADGEYE KLANEALFAA AADTTVSKDR VLTPREIYDG LNEYVIGQDK VKKTLAVGVH
NHYKRLHALE LLQARKEAEA ACAKHNASSQ HPRAGGVTRQ HVDMDDSRLS SIGRRLLLEE
IYPGSEKNDA EVPQNSKQHA SEETAEAPKT TETTHTHATR LQHHSLGDKL QYLEGVELDK
TNVMLVGPTG SGKTLLAKTL ARLAKVPIVI ADATCLTQAG YVGEDVESVL FKLYQAANYN
LEATQRGIVY IDEIDKITRK SENVSITRDV SGEGVQQALL KILEGSMVNV PEKGGRKNPR
GEYITIDTTN ILFICGGAFA GLEKQVTRRT SRSSIGFGAQ MPNMRLKDSD QIGQLLSQAE
PEDLVSYGLI PEFIGRFPML VSTTGLSKDE LVQVLTEPKN SLVRQYKALF ALSDVEFHAT
EGALEAVAES ALRKNTGARG LRSIFERALM ETMFELPDMN DVRAVYVDEE AILGRKRPVL
IRGEMTLDEY LKNLEDDSDK REEAV
//