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FTSH_THET8
ID   FTSH_THET8              Reviewed;         624 AA.
AC   Q5SI82; Q9LCZ4;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=TTHA1492;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, ATPASE ACTIVITY,
RP   PROCESSIVE PROTEASE ACTIVITY, ACTIVITY REGULATION, AND ZINC COFACTOR.
RX   PubMed=10788805; DOI=10.1093/oxfordjournals.jbchem.a022689;
RA   Asahara Y., Atsuta K., Motohashi K., Taguchi H., Yohda M., Yoshida M.;
RT   "FtsH recognizes proteins with unfolded structure and hydrolyzes the
RT   carboxyl side of hydrophobic residues.";
RL   J. Biochem. 127:931-937(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RX   PubMed=10377389; DOI=10.1073/pnas.96.13.7184;
RA   Motohashi K., Watanabe Y.H., Yohda M., Yoshida M.;
RT   "Heat-inactivated proteins are rescued by the DnaK/J-GrpE set and ClpB
RT   chaperones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7184-7189(1999).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 146-393 WITHOUT NUCLEOTIDE,
RP   COMPLEXED WITH ADP OR AMP-PNP, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF
RP   126-393, AND POSSIBLE SUBUNIT.
RX   PubMed=12377127; DOI=10.1016/s0969-2126(02)00855-9;
RA   Niwa H., Tsuchiya D., Makyio H., Yoshida M., Morikawa K.;
RT   "Hexameric ring structure of the ATPase domain of the membrane-integrated
RT   metalloprotease FtsH from Thermus thermophilus HB8.";
RL   Structure 10:1415-1423(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.9 ANGSTROMS) OF 126-624, SUBUNIT, MUTAGENESIS OF
RP   GLY-399, PROTEOLYTIC ACTIVITY, AND ATP-DEPENDENCE.
RX   PubMed=16762831; DOI=10.1016/j.molcel.2006.04.020;
RA   Suno R., Niwa H., Tsuchiya D., Zhang X., Yoshida M., Morikawa K.;
RT   "Structure of the whole cytosolic region of ATP-dependent protease FtsH.";
RL   Mol. Cell 22:575-585(2006).
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   -!- FUNCTION: Degrades preferentially unfolded substrates in a processive,
CC       ATP-dependent manner, usually after hydrophobic residues.
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   -!- ACTIVITY REGULATION: The proteolytic activity is dependent on ATP, both
CC       the ATPase and protease activities are inhibited by ADP.
CC       {ECO:0000269|PubMed:10788805}.
CC   -!- SUBUNIT: The isolated soluble domain (residues 126-624) forms a stable
CC       hexamer in which the AAA+ domains (residues 126-400) are alternatively
CC       open or closed. {ECO:0000269|PubMed:16762831}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:10788805}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_01458}.
CC   -!- DOMAIN: The open AAA+ domain (residues 126-400) probably allows
CC       nucleotide exchange and has the protease active site, while the closed
CC       domain is the active ATPase domain but the protease is inactive.
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; AB032368; BAA96090.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD71315.1; -; Genomic_DNA.
DR   EMBL; AB012390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_011173542.1; NC_006461.1.
DR   RefSeq; YP_144758.1; NC_006461.1.
DR   PDB; 1IXZ; X-ray; 2.20 A; A=146-393.
DR   PDB; 1IY0; X-ray; 2.95 A; A=146-393.
DR   PDB; 1IY1; X-ray; 2.80 A; A=146-393.
DR   PDB; 1IY2; X-ray; 3.20 A; A=126-393.
DR   PDB; 2DHR; X-ray; 3.90 A; A/B/C/D/E/F=126-624.
DR   PDB; 4EIW; X-ray; 3.90 A; A/B/C/D/E/F=126-624.
DR   PDBsum; 1IXZ; -.
DR   PDBsum; 1IY0; -.
DR   PDBsum; 1IY1; -.
DR   PDBsum; 1IY2; -.
DR   PDBsum; 2DHR; -.
DR   PDBsum; 4EIW; -.
DR   AlphaFoldDB; Q5SI82; -.
DR   SMR; Q5SI82; -.
DR   STRING; 300852.55772874; -.
DR   MEROPS; M41.013; -.
DR   PRIDE; Q5SI82; -.
DR   EnsemblBacteria; BAD71315; BAD71315; BAD71315.
DR   GeneID; 3170023; -.
DR   KEGG; ttj:TTHA1492; -.
DR   PATRIC; fig|300852.9.peg.1467; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_2_0; -.
DR   OMA; YDKQGGG; -.
DR   PhylomeDB; Q5SI82; -.
DR   BRENDA; 3.4.24.B17; 2305.
DR   EvolutionaryTrace; Q5SI82; -.
DR   Proteomes; UP000000532; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..624
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /id="PRO_0000400413"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        29..103
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        125..624
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   REGION          595..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         199..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
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         493
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   MUTAGEN         399
FT                   /note="G->L: No effect on protease activity against alpha-
FT                   casein."
FT                   /evidence="ECO:0000269|PubMed:16762831"
FT   CONFLICT        21..25
FT                   /note="AFSLA -> PSASR (in Ref. 1; BAA96090 and 2;
FT                   AB012390)"
FT                   /evidence="ECO:0000305"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:1IY2"
FT   HELIX           162..176
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           178..183
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          190..195
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:1IY1"
FT   HELIX           202..212
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          217..221
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           222..227
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   TURN            229..231
FT                   /evidence="ECO:0007829|PDB:1IY2"
FT   HELIX           232..244
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          247..255
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           257..261
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           273..287
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          295..302
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           309..312
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          319..322
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           328..339
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           350..355
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           362..378
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   STRAND          382..384
FT                   /evidence="ECO:0007829|PDB:1IXZ"
FT   HELIX           386..392
FT                   /evidence="ECO:0007829|PDB:1IXZ"
SQ   SEQUENCE   624 AA;  68452 MW;  A2000075F32E3A6F CRC64;
     MPRAPFSLLA LVLGLAFLAW AFSLAGTVGA PSGTVNYTTF LEDLKAGRVK EVVVRAGDTR
     IQGVLEDGSA FTTYAASPPD NATLEGWMAR GVSVRVEPPQ GQNALGFLWP LLLVGLLIGA
     LYYFSRNGRA GPSDSAFSFT KSRARVLTEA PKVTFKDVAG AEEAKEELKE IVEFLKNPSR
     FHEMGARIPK GVLLVGPPGV GKTHLARAVA GEARVPFITA SGSDFVEMFV GVGAARVRDL
     FETAKRHAPC IVFIDEIDAV GRKRGSGVGG GNDEREQTLN QLLVEMDGFE KDTAIVVMAA
     TNRPDILDPA LLRPGRFDRQ IAIDAPDVKG REQILRIHAR GKPLAEDVDL ALLAKRTPGF
     VGADLENLLN EAALLAAREG RRKITMKDLE EAADRVMMGP AKKSLVLSPR DRRITAYHEA
     GHALAAHFLE HADGVHKVTI VPRGRALGFM MPRREDMLHW SRKRLLDQIA VALAGRAAEE
     IVFDDVTTGA ENDFRQATEL ARRMITEWGM HPEFGPVAYA VREDTYLGGY DVRQYSEETA
     KRIDEAVRRL IEEQYQRVKA LLLEKREVLE RVAETLLERE TLTAEEFQRV VEGLPLEAPE
     EAREEREPPR VVPKVKPGGA LGGA
 
 
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