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FTSH_SALTY
ID   FTSH_SALTY              Reviewed;         644 AA.
AC   P63343; Q8XGY2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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}; Synonyms=hflB;
GN   OrderedLocusNames=STM3296;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL22166.1; -; Genomic_DNA.
DR   RefSeq; NP_462207.1; NC_003197.2.
DR   RefSeq; WP_001107481.1; NC_003197.2.
DR   AlphaFoldDB; P63343; -.
DR   SMR; P63343; -.
DR   STRING; 99287.STM3296; -.
DR   MEROPS; M41.001; -.
DR   PaxDb; P63343; -.
DR   PRIDE; P63343; -.
DR   EnsemblBacteria; AAL22166; AAL22166; STM3296.
DR   GeneID; 1254819; -.
DR   GeneID; 66757635; -.
DR   KEGG; stm:STM3296; -.
DR   PATRIC; fig|99287.12.peg.3494; -.
DR   HOGENOM; CLU_000688_16_0_6; -.
DR   OMA; QYGMTER; -.
DR   PhylomeDB; P63343; -.
DR   BioCyc; SENT99287:STM3296-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..644
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /id="PRO_0000084648"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        26..98
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        120..644
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   REGION          599..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         192..199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         492
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   644 AA;  70829 MW;  0F4195A2CB40CF98 CRC64;
     MAKNLILWLV IAVVLMSVFQ SFGPSESNGR KVDYSTFLQE VNQDQVREAR INGREINVTK
     KDSNRYTTYI PINDPKLLDN LLTKNVKVVG EPPEEPSLLA SIFISWFPML LLIGVWIFFM
     RQMQGGGGKG AMSFGKSKAR MLTEDQIKTT FADVAGCDEA KEEVAELVEY LREPSRFQKL
     GGKIPKGVLM VGPPGTGKTL LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEQA
     KKAAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFEGNEG IIVIAATNRP
     DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL ATDIDAAIIA RGTPGFSGAD
     LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS MVMTEAQKES TAYHEAGHAI
     IGRLVPEHDP VHKVTIIPRG RALGVTFFLP EGDAISASRQ KLESQISTLY GGRLAEEIIY
     GVEHVSTGAS NDIKVATNLA RNMVTQWGFS EKLGPLLYAE EEGEVFLGRS VAKAKHMSDE
     TARIIDQEVK ALIERNYNRA RQILTDNMDI LHAMKDALMK YETIDAPQID DLMARREVRP
     PAGWEDPNGT NNSDSNGTPQ APRPVDEPRT PNPGNTMSEQ LGDK
 
 
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