ID A0A067CCP3_SAPPC Unreviewed; 478 AA.
AC A0A067CCP3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Heat shock protein HslVU {ECO:0000313|EMBL:KDO24306.1};
GN ORFNames=SPRG_10381 {ECO:0000313|EMBL:KDO24306.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO24306.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO24306.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO24306.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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DR EMBL; KK583243; KDO24306.1; -; Genomic_DNA.
DR RefSeq; XP_012204903.1; XM_012349513.1.
DR AlphaFoldDB; A0A067CCP3; -.
DR STRING; 695850.A0A067CCP3; -.
DR EnsemblProtists; KDO24306; KDO24306; SPRG_10381.
DR GeneID; 24132495; -.
DR KEGG; spar:SPRG_10381; -.
DR VEuPathDB; FungiDB:SPRG_10381; -.
DR OMA; CMQKTFD; -.
DR OrthoDB; 48707at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004491; HslU.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00390; hslU; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Stress response {ECO:0000313|EMBL:KDO24306.1}.
FT DOMAIN 85..371
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 370..464
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 478 AA; 52897 MW; 2082EB38AE40BC08 CRC64;
MFIQRTRFLG RTHAHQGTKA FSSFMLVDPK ASNPDASMEL TPEQVVYQLD QHIIGQTDAK
KAVAIALRNR WRRRQLDGPM RSEISPMNIL MSGPTGSGKT EIARRLAKLT QSPFVKVEAT
KFTEVGVYGS NADSMIKDLT DIAIDMEREA AKKANASAAR ARAIERVLDL IAPAHSSSDA
LRRKLRADIA SGDADDRLIT VVLKPIESTH RRRGSPEDMM MELPPELQQM MKQLSGVLGA
RDGQPKKQGQ TMTVKEALPK LEAEEAVSGL NEDDIVQRAI ENVQTNGIVF LDEVDKLAQN
NDNRSFRKGE GVQKELLALT EGCAVHTRHG IVHTDHILFI ASGAFHNCSP SDLMPELQGR
LPIRVNLSPL TEKDFVRILT ETQYNLLDQV RALMATEDVS VVFTDDAIDE IASISAQVNV
QTDNIGARRL ATVVAKITEH VSFHAPSLKA STVTIDKAYV QEHLKDILQK TDLTKYIL
//