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FTSH_ENDTX
ID   FTSH_ENDTX              Reviewed;         631 AA.
AC   B1GZK7;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE            EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN   Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=TGRD_206;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for
CC       both cytoplasmic and membrane proteins. Plays a role in the quality
CC       control of integral membrane proteins. {ECO:0000255|HAMAP-
CC       Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR   EMBL; AP009510; BAG13689.1; -; Genomic_DNA.
DR   RefSeq; WP_015423217.1; NC_020419.1.
DR   RefSeq; YP_001956150.1; NC_020419.1.
DR   AlphaFoldDB; B1GZK7; -.
DR   SMR; B1GZK7; -.
DR   STRING; 471821.TGRD_206; -.
DR   MEROPS; M41.021; -.
DR   EnsemblBacteria; BAG13689; BAG13689; TGRD_206.
DR   KEGG; rsd:TGRD_206; -.
DR   PATRIC; fig|471821.5.peg.312; -.
DR   HOGENOM; CLU_000688_16_2_0; -.
DR   OMA; QYGMTER; -.
DR   OrthoDB; 190468at2; -.
DR   Proteomes; UP000001691; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..631
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /id="PRO_0000400416"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        27..102
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        124..631
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         196..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         422
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         494
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   631 AA;  69800 MW;  BC8720BCCF670C06 CRC64;
     MKKSNPWFVF FWITLLVIVL MFINFARQGG NEVELEYSQF KQHIKAGSVF KVLVAPGLIR
     GQFRDGDGVF KRFKTVPMDD PNLVKDMEDN KVLEFSATEK SGWLGSLLLN WGPVVLLILF
     CFWMMRGMSM GNKQAMSFGK TKAKLAVGAS KKITFKDVAG CDEAKEELQE LIEFLKDPAR
     FQKLGGKIPK GVLLFGSPGT GKTLLAKAVA GEANVPFFSS SGSEFVEMFV GVGASRVRDL
     FDHGRKSAPC LLFIDEIDAV GRHRFAGIGG GHDEREQTLN QLLVEMDGFD SKEGVILIAA
     TNRPDVLDPA LLRPGRFDRQ VIILSPDLKD REEILGVHSK KIRLDNDVNL NVIARRTPGF
     VGADLANLVN EAALLAARNS QNAVNMKNME EAIDRILAGP QRKSRLMSDK EKNIIAYHEA
     GHTLVAKFLP SADPVHKVSI IPRGPALGYT LQLPEEDKYL TSKSELLDKL SILFGGRVAE
     ELVFSEITTG AQNDISKATG IAMRMVTEFG MSDKIGPMAL QRPNEEVFLG RDISRDARHS
     GKTSELIDEE VKNIIYSSKS RASKIIKDNV SILNKIVSYL LERENLSGED IDKIIKGEEL
     APLSESSSVD EETKKKSTVE KKVINEKVII S
 
 
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