ID Q6MTI5_MYCMS Unreviewed; 447 AA. AC Q6MTI5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 14-DEC-2022, entry version 123. DE RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306, GN ECO:0000313|EMBL:CAE77051.1}; GN ORFNames=MSC_0423 {ECO:0000313|EMBL:CAE77051.1}; OS Mycoplasma mycoides subsp. mycoides SC (strain PG1). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=272632 {ECO:0000313|EMBL:CAE77051.1, ECO:0000313|Proteomes:UP000001016}; RN [1] {ECO:0000313|EMBL:CAE77051.1, ECO:0000313|Proteomes:UP000001016} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG1 {ECO:0000313|EMBL:CAE77051.1, RC ECO:0000313|Proteomes:UP000001016}; RX PubMed=14762060; DOI=10.1101/gr.1673304; RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J., RA Johansson K.-E., Pettersson B., Uhlen M.; RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP)."; RL Genome Res. 14:221-227(2004). 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 {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SUBUNIT: Part of the signal recognition particle protein translocation CC system, which is composed of SRP and FtsY. {ECO:0000256|HAMAP- CC Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily. CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|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; BX293980; CAE77051.1; -; Genomic_DNA. DR RefSeq; NP_975409.1; NC_005364.2. DR AlphaFoldDB; Q6MTI5; -. DR STRING; 272632.MSC_0423; -. DR EnsemblBacteria; CAE77051; CAE77051; MSC_0423. DR KEGG; mmy:MSC_0423; -. DR PATRIC; fig|272632.4.peg.461; -. DR eggNOG; COG0541; Bacteria. DR HOGENOM; CLU_009301_6_0_14; -. DR OMA; DTAGRHK; -. DR Proteomes; UP000001016; 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: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; 1.10.260.30; -; 1. DR Gene3D; 1.20.120.140; -; 1. DR Gene3D; 3.40.50.300; -; 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; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR042101; SRP54_N_sf. DR PANTHER; PTHR11564:SF7; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN, CHLOROPLASTIC; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47446; Signal peptide-binding domain; 1. DR TIGRFAMs; TIGR00959; ffh; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00306}; Reference proteome {ECO:0000313|Proteomes:UP000001016}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135, KW ECO:0000256|HAMAP-Rule:MF_00306}. FT DOMAIN 269..282 FT /note="SRP54" FT /evidence="ECO:0000259|PROSITE:PS00300" FT BINDING 108..115 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT BINDING 190..194 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT BINDING 248..251 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" SQ SEQUENCE 447 AA; 50161 MW; D27FE990C7FDD479 CRC64; MGFGDFLSKR MQKSIEKNMK NSTLNEENIK ETLKEIRLSL LEADVNIEAT KEIINNVKQK ALGGYIFEGA NAHQQMIKIV HEELVNILGK ENAPLELNKK PSVVMMVGLQ GSGKTTTANK LAYLLNKKNK KKVLLVGLDI YRPGAIEQLI QLGQKTNIQV FEKGKQDPIL TAQEALEYAQ ENNFDVVILD TAGRLQVDQV LMTELDNLKK KTSPSEILLV VDGMSGQEII NVTNEFNSKL KLSGVVVTKL DGDARGGATL SISYLTKLPI KFIGEGEGYN ALAAFYPKRM ADRLMGMGDI ETLFEKAVEN IDERSIQKTM NRMFLGQFDL EDLRNQLAQI AKMGSLNKLM KMLPINKVSE TQIQDAQRKL AVFSILMDSM TLKERRDPRV LKAISRKNRI IKGSGRTEKE FNELINSFEK GKKQVLEITK MIKSGRMPNL SKGGFKF //