AC MF_00306; DC Protein; auto TR HAMAP; MF_00306; -; 1; level=0 XX Names: SRP54 XX ID SRP54 case DE RecName: Full=Signal recognition particle 54 kDa protein; DE Short=SRP54; DE EC=3.6.5.4; GN Name=srp54; else case DE RecName: Full=Signal recognition particle protein; DE EC=3.6.5.4; DE AltName: Full=Fifty-four homolog; GN Name=ffh; end case XX case CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic signal CC sequence of the ribosome-nascent chain (RNC) as it emerges from the CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic CC membrane where it interacts with the SRP receptor FtsY. 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. Archaeal SRP consists of a CC 7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and CC SRP19. else case CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic signal CC sequence of the ribosome-nascent chain (RNC) as it emerges from the CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic CC membrane where it interacts with the SRP receptor FtsY. Interaction CC with FtsY leads to the transfer of the RNC complex to the Sec CC translocase for insertion into the membrane, the hydrolysis of GTP by CC both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into CC 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. Binds to the hydrophobic signal CC sequence of the ribosome-nascent chain (RNC) as it emerges from the CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic CC membrane where it interacts with the SRP receptor FtsY. 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 CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=The SRP-RNC complex is targeted CC to the cytoplasmic membrane. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which is CC responsible for interactions with the ribosome, the central G domain, CC which binds GTP, and the C-terminal M domain, which binds the RNA and CC the signal sequence of the RNC. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily. XX DR Pfam; PF00448; SRP54; 1; trigger=no DR Pfam; PF02881; SRP54_N; 1; trigger=no DR Pfam; PF02978; SRP_SPB; 1; trigger=no DR PROSITE; PS00300; SRP54; 1; trigger=no DR NCBIfam; TIGR00959; Ffh; 1; trigger=no XX KW Cytoplasm KW Signal recognition particle KW GTP-binding KW Hydrolase KW Nucleotide-binding KW Ribonucleoprotein KW RNA-binding XX GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity case GO GO:0008312; F:7S RNA binding else case GO GO:0003723; F:RNA binding end case GO GO:0006612; P:protein targeting to membrane GO GO:0048500; C:signal recognition particle GO GO:1990904; C:ribonucleoprotein complex XX FT From: SRP54_METJA (Q57565) FT BINDING 107..114 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: G-x-x-G-x(1,3)-G-K-T FT BINDING 188..192 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: D-[ST]-[AS]-G-R FT BINDING 247..250 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: x-[KR]-x-D XX Size: 430-525; Related: None; Template: P0AGD7; O29633; P37105; O07347; Q977V2; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.35 2023/06/01 //