ID M2WVF7_GALSU Unreviewed; 548 AA.
AC M2WVF7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=ATP-dependent HslUV protease ATP-binding subunit HslU {ECO:0000313|EMBL:EME27965.1};
GN ORFNames=Gasu_44710 {ECO:0000313|EMBL:EME27965.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27965.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771}.
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DR EMBL; KB454525; EME27965.1; -; Genomic_DNA.
DR RefSeq; XP_005704485.1; XM_005704428.1.
DR AlphaFoldDB; M2WVF7; -.
DR STRING; 130081.M2WVF7; -.
DR EnsemblPlants; EME27965; EME27965; Gasu_44710.
DR GeneID; 17086841; -.
DR Gramene; EME27965; EME27965; Gasu_44710.
DR KEGG; gsl:Gasu_44710; -.
DR eggNOG; KOG0745; Eukaryota.
DR OMA; KYGMIKT; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19498; RecA-like_HslU; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
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 ATP-binding {ECO:0000313|EMBL:EME27965.1};
KW Hydrolase {ECO:0000313|EMBL:EME27965.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EME27965.1};
KW Protease {ECO:0000313|EMBL:EME27965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT DOMAIN 166..441
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 440..534
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 548 AA; 61253 MW; D07BBC259A844868 CRC64;
MFPQRLWLGC NKVVQQLQKS GTQKTVAVYS STTQRYCFGP IERLPITSKK YGLPNKLYNS
TTSRVPITNH KSWDGFLRNF STDTSSSDGA NNKVPVPVSP VINVEDNQGN DNGATKAPRE
LTPKEIVAEL DKFIVGQTEA KRAMAIALRN RWRRHHVVKE LADEVIPKNI LMIGPTGVGK
TEIARRLAKL VDAPFVKVEA TKYTEVGFHG RDVDQIIRDL VENAVQMVKA KKRREIKETV
DKLVEERILD ELTGPQARKE TRESFRNLLR KGALEDREIE VPESGKNKSP HVVQMGDVMP
EIFNLEKIFT MSKSGGKKRM KVKDARQVLE DMESDKLLSD ESVIQQAIQL TEQDGIVFID
EIDKICTPNG WRSGADASAE GVQRDLLPLI EGSTISTKYG NVDTEHILFV ASGAFHQCKP
SDLMAELQGR LPIRVELKGL SENDLYQILT VPVNNLIRQQ VELMKTEGVN LVFTPDAIRE
IAAVAAEVNT NVENIGARRL YTVIERIVED ISFNAPDWKG QTVTIDAPSV KGSLGDMLLK
TDLSKFVL
//