ID A0A3T4RMW8_SALET Unreviewed; 491 AA. AC A0A3T4RMW8; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 05-JUN-2019, entry version 2. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920, GN ECO:0000313|EMBL:EAA8802791.1}; GN ORFNames=AH874_15245 {ECO:0000313|EMBL:EAA8802791.1}, D5810_06595 GN {ECO:0000313|EMBL:EAB7705854.1}, D6J84_03320 GN {ECO:0000313|EMBL:EAB9906141.1}, DK681_02270 GN {ECO:0000313|EMBL:EAA1055528.1}, DOQ73_08630 GN {ECO:0000313|EMBL:EAA3796403.1}, DQJ71_07670 GN {ECO:0000313|EMBL:EAA5641988.1}, EHD17_03595 GN {ECO:0000313|EMBL:EAC0179524.1}, ZG82_03405 GN {ECO:0000313|EMBL:EAB5676250.1}; OS Salmonella enterica I. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=59201 {ECO:0000313|EMBL:EAA1055528.1}; RN [1] {ECO:0000313|EMBL:EAA1055528.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=257392 {ECO:0000313|EMBL:EAA3796403.1}, 285874 RC {ECO:0000313|EMBL:EAB7705854.1}, 305271 RC {ECO:0000313|EMBL:EAA5641988.1}, 476611 RC {ECO:0000313|EMBL:EAA1055528.1}, 600747 RC {ECO:0000313|EMBL:EAB9906141.1}, 638782 RC {ECO:0000313|EMBL:EAC0179524.1}, and 83589 RC {ECO:0000313|EMBL:EAB5676250.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAA8802791.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FDA00002754 {ECO:0000313|EMBL:EAA8802791.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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 CC the transfer of the RNC complex to the Sec translocase for CC insertion into the membrane, the hydrolysis of GTP by both Ffh and CC FtsY, and the dissociation of the SRP-FtsY complex into the CC individual components. {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. SRP is a CC ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. CC {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00920}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00920}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_00920}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- DOMAIN: Contains an acidic N-terminal A domain, a central N domain CC and a C-terminal GTPase G domain that can bind and hydrolyze GTP. CC Contains at least two lipid-binding sites. The first site contains CC the first 14 amino acids (helix 1) and the second binding site is CC an amphipathic alpha-helix located at the interface between the A- CC and the N-domain (helix 2). {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAA1055528.1}. 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; AAAALO010000007; EAA1055528.1; -; Genomic_DNA. DR EMBL; AAABHZ010000004; EAA3796403.1; -; Genomic_DNA. DR EMBL; AAABWX010000004; EAA5641988.1; -; Genomic_DNA. DR EMBL; AAACWI010000006; EAA8802791.1; -; Genomic_DNA. DR EMBL; AAAFCJ010000002; EAB5676250.1; -; Genomic_DNA. DR EMBL; AAAFTD010000003; EAB7705854.1; -; Genomic_DNA. DR EMBL; AAAGKJ010000002; EAB9906141.1; -; Genomic_DNA. DR EMBL; AAAGNQ010000002; EAC0179524.1; -; Genomic_DNA. DR RefSeq; WP_001528170.1; NZ_QAPU01000004.1. DR Gene3D; 1.20.120.140; -; 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 PANTHER; PTHR43134:SF7; PTHR43134:SF7; 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; SSF47364; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00064; ftsY; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Receptor {ECO:0000256|HAMAP-Rule:MF_00920}. FT DOMAIN 461 474 SRP54. {ECO:0000259|PROSITE:PS00300}. FT NP_BIND 294 301 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT NP_BIND 376 380 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT NP_BIND 440 443 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT REGION 1 58 Disordered. {ECO:0000256|MobiDB-lite: FT A0A3T4RMW8}. FT REGION 70 89 Disordered. {ECO:0000256|MobiDB-lite: FT A0A3T4RMW8}. FT COILED 384 404 {ECO:0000256|SAM:Coils}. FT COMPBIAS 19 33 Polyampholyte. {ECO:0000256|MobiDB-lite: FT A0A3T4RMW8}. SQ SEQUENCE 491 AA; 53777 MW; 1D43F7DB77B2D8E3 CRC64; MAKQKKRGFF SWLGFGDKEQ KQEQTEEQQI VEEQRPVEPP VETAADIDAQ TPAHSKAETE AFAEEVVDVT EKVQESEKPQ PVEPEPATAV ETAAPQIAVE REELLLPEEV KDEAISPEEW QAEAETVEVI AAVEEEGENA AKFTDEELEA QALAAQAAEE AVMVVPPAEE DAPVEAIVQE QEKPTKEGFF ARLKRSLLKT KENLGSGFIS LFRGKKIDDD LFEELEEQLL IADVGVETTR KIIANLTEGA SRKQLKDAEA LYGLLKDEMG EILAKVDEPL NIEGKTPFVI LMVGVNGVGK TTTIGKLARQ FEQQGKSVML AAGDTFRAAA VEQLQVWGQR NNIPVIAQHT GADSASVIFD AIQAAKARNV DVLIADTAGR LQNKSHLMEE LKKIVRVMKK LDEEAPHEVM LTIDASTGQN AVSQAKLFHE AVGLTGITLT KLDGTAKGGV IFSVADQFGI PIRYIGVGER IEDLRPFKAD DFIEALFARE D //