ID FTSY_BUCAP Reviewed; 351 AA. AC Q8KA77; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, 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}; DE EC=3.6.5.4 {ECO:0000255|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; GN OrderedLocusNames=BUsg_025; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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 -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4; CC Evidence={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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE013218; AAM67596.1; -; Genomic_DNA. DR RefSeq; WP_011053562.1; NC_004061.1. DR AlphaFoldDB; Q8KA77; -. DR SMR; Q8KA77; -. DR STRING; 198804.BUsg_025; -. DR GeneID; 75259107; -. DR KEGG; bas:BUsg_025; -. DR eggNOG; COG0552; Bacteria. DR HOGENOM; CLU_009301_3_0_6; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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 CDD; cd17874; FtsY; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 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 NCBIfam; TIGR00064; ftsY; 1. DR PANTHER; PTHR43134:SF7; CELL DIVISION PROTEIN FTSY HOMOLOG, CHLOROPLASTIC; 1. DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 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; Domain of the SRP/SRP receptor G-proteins; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Membrane; KW Nucleotide-binding; Receptor. FT CHAIN 1..351 FT /note="Signal recognition particle receptor FtsY" FT /id="PRO_0000101129" FT BINDING 156..163 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920" FT BINDING 238..242 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920" FT BINDING 302..305 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920" SQ SEQUENCE 351 AA; 39470 MW; 1CA5A59A4B6E7FF3 CRC64; MNFDKKNSFF SWINSKIKKN NKKEKKENIL LKKEKEGIHT IQNIDNKKID FLFKLKNSLN KTKQFFGDSI SRIFLSKKID DAFFEELEDT MLLSDIGVHT TDQIISKLIN DATHKELKNP EKVYFLLKEH MYSILNRVEK PLKISNHTPF VILVVGINGT GKTTTVSKLA KKYKLAGKSV MLAAADTFRA AGIEQLQILG KRNNIPVISQ SSGSDPASVA FDAVKSAISK KIDVLIIDTA GRLHNKLHLL EELKKMVRVI KKLNLSAPHE IMLIIDACNG QNTIKQTEMF HKAINLTGLV ITKLDGTAKG GVIFSLANQF LIPIRYIGIG EKTTDLVVFN SNDFIKSIFV K //