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Database: UniProt
Entry: M2WVF7_GALSU
LinkDB: M2WVF7_GALSU
Original site: M2WVF7_GALSU 
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
//
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