AC MF_00920; DC Protein; auto TR HAMAP; MF_00920; -; 1; level=0 XX Names: FtsY XX ID FTSY DE RecName: Full=Signal recognition particle receptor FtsY; DE Short=SRP receptor; DE EC=3.6.5.4; GN Name=ftsY; XX case 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 -!- 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 -!- 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. else 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). 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 -!- SUBUNIT: Part of the signal recognition particle protein translocation CC system, which is composed of SRP and FtsY. end case case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm. end case case or or CC -!- DOMAIN: Contains an acidic N-terminal A domain, a central N domain and CC a C-terminal GTPase G domain that can bind and hydrolyze GTP. Contains CC at least two lipid-binding sites. The first site contains the first 14 CC amino acids (helix 1) and the second binding site is an amphipathic CC alpha-helix located at the interface between the A- and the N-domain CC (helix 2). end case CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. XX DR PROSITE; PS00300; SRP54; 1; trigger=no DR Pfam; PF00448; SRP54; 1; trigger=no DR Pfam; PF02881; SRP54_N; 1; trigger=no DR NCBIfam; TIGR00064; FtsY; 1; trigger=no XX case defined and KW Cell inner membrane end case KW Cell membrane KW Cytoplasm KW GTP-binding KW Hydrolase KW Membrane KW Nucleotide-binding KW Receptor XX GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity GO GO:0006612; P:protein targeting to membrane GO GO:0005737; C:cytoplasm GO GO:0005886; C:plasma membrane XX FT From: FTSY_ECOLI (P10121) FT BINDING 300..307 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Optional; Condition: G-x-N-G-x-G-K-T FT BINDING 382..386 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Optional; Condition: D-[TS]-[AS]-G-R FT BINDING 446..449 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Optional; Condition: [TS]-K-x-[DE] XX Size: 288-504; Related: None; Template: P10121; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.10 2023/06/01 //