ID A0A2G4SKA8_RHIZD Unreviewed; 566 AA.
AC A0A2G4SKA8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE SubName: Full=ClpX, ATPase regulatory subunit {ECO:0000313|EMBL:PHZ09172.1};
GN ORFNames=RHIMIDRAFT_246456 {ECO:0000313|EMBL:PHZ09172.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ09172.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ09172.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ09172.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303860; PHZ09172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4SKA8; -.
DR STRING; 1340429.A0A2G4SKA8; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000242254; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0051082; F:unfolded protein binding; IEA:InterPro.
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; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000242254}.
FT DOMAIN 222..390
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"
FT REGION 111..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 62590 MW; E62D6F16106957B4 CRC64;
MKYMRMLTLY RPVLATTVLR PSIVRLPIRA YHNAEYNGGG LMGIDNFPVQ PPTKGFDHPF
SQLEFSHLNN PRAIVKHLNE YVIGQERAKK ILAVAIFNHY NRVRANMKRQ YLQQQKHDSV
EGDSPIEHHH PSVPHDNYYA VNHLPLQSNN NNNNNNNNNT NNSSELSGPI SSTGYSNGSQ
RRAWLNPPTE GHSNMDSKHT YHDESELGSI LELNDQDTTV HDKSNVLLIG PTGSGKTLLA
RTLAQILQVP FSMSDATPFT QAGYVGEDVE LVIQRLLQAC DFDVKKAETG IVFIDEIDKI
SRRSDAHTAS RDVSGEGVQQ SLLRMLEGTI VNVTDKSGAG HHKRGSPTGG NGAGGSSKGE
TYSVDTSNIL FILSGAFIGL DKIISERVAK GSIGFGAHLK SENESTKDTL HAVEPADLIK
YGFIPEFVGR IPVVASVNNL EVHDLVRVLK EPKNSLLKQY EGLFKLNNVQ LRFSQNALRS
VAAQALEKKT GARGLRRIME NILLEPMYDT PGSCIKQVII DSKVVNKEKS PIYITTEKSP
LADKIVAEDD GIDLTEDDTQ QQMTQI
//