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FTSY_BUCAI
ID   FTSY_BUCAI              Reviewed;         378 AA.
AC   P57137;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=BU024;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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 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; BA000003; BAB12751.1; -; Genomic_DNA.
DR   RefSeq; NP_239865.1; NC_002528.1.
DR   RefSeq; WP_010895906.1; NC_002528.1.
DR   AlphaFoldDB; P57137; -.
DR   SMR; P57137; -.
DR   STRING; 107806.10038716; -.
DR   EnsemblBacteria; BAB12751; BAB12751; BAB12751.
DR   KEGG; buc:BU024; -.
DR   PATRIC; fig|107806.10.peg.36; -.
DR   eggNOG; COG0552; Bacteria.
DR   HOGENOM; CLU_009301_3_0_6; -.
DR   OMA; GISDQFQ; -.
DR   Proteomes; UP000001806; 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 membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW   Receptor; Reference proteome.
FT   CHAIN           1..378
FT                   /note="Signal recognition particle receptor FtsY"
FT                   /id="PRO_0000101128"
FT   BINDING         184..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         266..270
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         330..333
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   378 AA;  42779 MW;  296119C0B36701BD CRC64;
     MKDSKKNGFF SWLSSKIKKK KTIDIRQNNT DKNHDINHED LYTKKDLLIK QDNPKKDEID
     TLNDHGKDIE KAQNTKNNFF LRLKKSLKTT KKNLGDKIYQ IFLSKKIDEV LFEELEEKML
     LADIGINTTN RIISNLIKDV NREDLKNSEK LYFLLKRKMF NILKKVEIPL EISSHSPFVI
     LVVGVNGTGK TTTVAKLAEK YKLEGKSIML AAADTFRAAG IEQLQTLGKL NNIPVIAQRS
     GSDPAAVIFD AVKSAKSKKI DVLIIDTAGR LHNKLHLIEE LKKIVRVIKK IDISAPHEKL
     LIIDSCNGQN TIQQTEIFHK ALNLTGIIIT KLDGTAKGGV VFSLADQFQI PIRYIGIGEK
     MQDLGHFNSQ EFIESIFT
 
 
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