ID SRP54_BUCAP Reviewed; 450 AA. AC Q8K9F7; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306}; DE EC=3.6.5.4 {ECO:0000255|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; GN OrderedLocusNames=BUsg_380; 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. 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. {ECO:0000255|HAMAP-Rule:MF_00306}. 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_00306}; 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_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000255|HAMAP-Rule:MF_00306}. 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. {ECO:0000255|HAMAP-Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00306}. 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; AAM67932.1; -; Genomic_DNA. DR RefSeq; WP_011053899.1; NC_004061.1. DR AlphaFoldDB; Q8K9F7; -. DR SMR; Q8K9F7; -. DR STRING; 198804.BUsg_380; -. DR GeneID; 75258741; -. DR KEGG; bas:BUsg_380; -. DR eggNOG; COG0541; Bacteria. DR HOGENOM; CLU_009301_6_0_6; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule. DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro. 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; cd18539; SRP_G; 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 Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR004780; SRP. DR InterPro; IPR036225; SRP/SRP_N. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR042101; SRP54_N_sf. DR NCBIfam; TIGR00959; ffh; 1. DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1. DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 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 SUPFAM; SSF47446; Signal peptide-binding domain; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Ribonucleoprotein; KW RNA-binding; Signal recognition particle. FT CHAIN 1..450 FT /note="Signal recognition particle protein" FT /id="PRO_0000101151" FT BINDING 107..114 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306" FT BINDING 190..194 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306" FT BINDING 248..251 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306" SQ SEQUENCE 450 AA; 51017 MW; 4A96BAFB8787D685 CRC64; MFNNLTERLS QSLRKIINKG RLTEENIKDT IREVRKALLE ADVTLSVIKK FIQNVSKKAI GHEINKSLTP GQEFIKIVKN ELILSMGEKN HDLNLSIQPP AIILVVGLQG VGKTTTLVKL AKWIKEKYKK KILTVSTDIY RAAAIKQLQI LSDQVKIDFY LSDTTQTPIN ITKEAIEHAK LKLYDLLLID TAGRLHINTE MMNEINTIQN ISKPIETLLI VDSMMGQDAI NIAKKFSASL SISGIVITKT DSDARSGVAL SIRHITGKPI KFIGTGEKLH QLEPFHPERI ADRILGMNQV ISLIKDIEEK VNQSQVKNLT KKFRKGDDFN LNDFLIQLKE MKNMGNLNYF IEKFSKNKIL SNNPLLGENK NTLNRIEAII YSMTHKERMH PIIIKGSRKR RIALGSGTKI QDVNKLLKNF DNIKKIMKKI KKGGIGKMIR NISNILPKNF //