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FTSY_RICPR
ID   FTSY_RICPR              Reviewed;         303 AA.
AC   O05948;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE            Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
GN   Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; OrderedLocusNames=RP775;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9274032; DOI=10.1099/00221287-143-8-2783;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genomic rearrangements during evolution of the obligate intracellular
RT   parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp
RT   nucleotide sequence.";
RL   Microbiology 143:2783-2795(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-303.
RC   STRAIN=B, and Madrid E;
RX   PubMed=10486973; DOI=10.1093/oxfordjournals.molbev.a026208;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genome degradation is an ongoing process in Rickettsia.";
RL   Mol. Biol. Evol. 16:1178-1191(1999).
CC   -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC       proteins into the cytoplasmic membrane. Acts as a receptor for the
CC       complex formed by the signal recognition particle (SRP) and the
CC       ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the
CC       transfer of the RNC complex to the Sec translocase for insertion into
CC       the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the
CC       dissociation of the SRP-FtsY complex into the individual components.
CC       {ECO:0000255|HAMAP-Rule:MF_00920}.
CC   -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC       system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein
CC       composed of Ffh and a 4.5S RNA molecule. {ECO:0000255|HAMAP-
CC       Rule:MF_00920}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR   EMBL; Y11784; CAA72477.1; -; Genomic_DNA.
DR   EMBL; AJ235273; CAA15202.1; -; Genomic_DNA.
DR   EMBL; AJ238755; CAB56084.1; -; Genomic_DNA.
DR   EMBL; AJ238756; CAB56088.1; -; Genomic_DNA.
DR   PIR; B71638; B71638.
DR   RefSeq; NP_221126.1; NC_000963.1.
DR   RefSeq; WP_004596957.1; NC_000963.1.
DR   AlphaFoldDB; O05948; -.
DR   SMR; O05948; -.
DR   STRING; 272947.RP775; -.
DR   EnsemblBacteria; CAA15202; CAA15202; CAA15202.
DR   GeneID; 57569898; -.
DR   KEGG; rpr:RP775; -.
DR   PATRIC; fig|272947.5.peg.810; -.
DR   eggNOG; COG0552; Bacteria.
DR   HOGENOM; CLU_009301_3_4_5; -.
DR   OMA; GISDQFQ; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   Gene3D; 1.20.120.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00920; FtsY; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR004390; SR_rcpt_FtsY.
DR   InterPro; IPR036225; SRP/SRP_N.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   PANTHER; PTHR43134:SF7; PTHR43134:SF7; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00962; SRP54; 1.
DR   SMART; SM00963; SRP54_N; 1.
DR   SUPFAM; SSF47364; SSF47364; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00064; ftsY; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Signal recognition particle receptor FtsY"
FT                   /id="PRO_0000101145"
FT   BINDING         108..115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         190..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         254..257
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   303 AA;  33314 MW;  BF3F7EB9383B7007 CRC64;
     MITIFNKLKQ SLSKTSNTIS AGIDKIFYKR KLDKETLNEL EELLISSDIS ISVVTHIIEE
     FKNVKFDKTI DSDTVKEAIA KLIEQQLSKS EIPFTLSENK LNIILVCGVN GVGKTTTIGK
     LSALYSAEGK KVAVAACDTF RAAAINQLSS WVHRANALLI TGKASADPAS VAYRAIEESI
     KQNIDILFID TAGRLHNNKN LMDELSKIVK VIKKLDENAP THSILIIDAI TGQNTYNQIE
     YFNDVTNLTG LIVTKLDGSA KAGVLVGAVQ KFNLPVYFIG IGEKIEDLKI FNRHDFSRSL
     VGL
 
 
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