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FTSH_MEDSA
ID   FTSH_MEDSA              Reviewed;         706 AA.
AC   Q9BAE0;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=FTSH;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ivashuta S., Imai R., Uchiyama K., Gau M., Shimamoto Y.;
RT   "Full length cDNA of alfalfa chloroplast FtsH protease.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Seems to act as an ATP-dependent zinc metallopeptidase.
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000305}.
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DR   EMBL; AF332134; AAK15322.1; -; mRNA.
DR   AlphaFoldDB; Q9BAE0; -.
DR   SMR; Q9BAE0; -.
DR   MEROPS; M41.020; -.
DR   PRIDE; Q9BAE0; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.760; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; SSF140990; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Chloroplast; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Plastid; Protease;
KW   Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..706
FT                   /note="ATP-dependent zinc metalloprotease FTSH,
FT                   chloroplastic"
FT                   /id="PRO_0000000246"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          74..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..89
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000250"
FT   BINDING         293..300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         515
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         519
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         595
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   706 AA;  75680 MW;  3645111C5929A010 CRC64;
     MAFSTSSLLS TNFLGARNIP TPKTTKPSIS LPLFFKTKFF NSQNDNNNNN SEPIKSAAVS
     ALILSSMFTP AALAADNLPP PPPPVLEAQP NQLNPANSTS PFSQNISLTA PKPQAQSSTD
     LPDGSQWRYS EFLNAVKKGK VERVRFSKDG SVLQLTAVDG RRANVIVPND PDLIDILAMN
     GVDISVSEGE QGNGLFSFVG SLLLPFLAFA GLFLIFRRGQ GGPGGPGGLG GPMDFGRSKS
     KFQEVPETGV TFADVAGADQ AKLELQEVVD FLKNPDKYTA LGAKIPKGCL LVGPPGTGKT
     LLARAVAGEA GTPFFSCAAS EFVELFVGVG ASRVRDLFEK AKSKAPCIVF IDEIDAVGRQ
     RGAGLGGGND EREQTINQLL TEMDGFSGNS GVIVLAATNR PDVLDSALLR PGRFDRQVTV
     DRPDVAGRVK ILQVHSRGKA LAKDVDFDKI ARRTPGFTGV DLQNLMNEAA ILAARRDLKE
     ISKDEIADAL ERIIAGPEKK NAVVSEEKKK LVAYHEAGHA LVGALMPEYD PVAKISIIPR
     GQAGGLTFFA PSEERLESGL YSRSYLENQM AVALGGRVAE EVFGQDNVTT GASNDFMQVS
     RVARQMVERF GFSKKIGQVA IGGGGGNPFL GQQMSSQKDY SMATADIVDK EVRELVDKAY
     ERATQIINTH IDILHKLAQL LIEKETVDGE EFMSLFIDGK AELYVS
 
 
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