ID A0A3T4RMW8_SALET Unreviewed; 491 AA. AC A0A3T4RMW8; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 24-JAN-2024, entry version 19. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920}; DE EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920, GN ECO:0000313|EMBL:EBP4056412.1}; GN ORFNames=DAX60_001355 {ECO:0000313|EMBL:QXR63995.1}, XB40_001410 GN {ECO:0000313|EMBL:QWI80807.1}, Z599_01310 GN {ECO:0000313|EMBL:EBP4056412.1}; OS Salmonella enterica I. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=59201 {ECO:0000313|EMBL:EBP4056412.1}; RN [1] {ECO:0000313|EMBL:QXR63995.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN058588 {ECO:0000313|EMBL:QXR63995.1}; RA Bell R.; RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EBP4056412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN001999 {ECO:0000313|EMBL:QWI80807.1}, and MDH-2013-00175 RC {ECO:0000313|EMBL:EBP4056412.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QWI80807.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN001999 {ECO:0000313|EMBL:QWI80807.1}; RA Hoffmann M., Balkey M., Luo Y.; RT "Whole genome PacBio Sequel sequence of Salmonella enterica subsp. RT enterica."; RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:QXR63995.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN058588 {ECO:0000313|EMBL:QXR63995.1}; RA Hoffmann M., Balkey M., Luo Y.; RT "Whole genome sequencing of cultured pathogen."; RL Submitted (MAY-2021) 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 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 {ECO:0000256|HAMAP-Rule:MF_00920}. 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:0000256|ARBA:ARBA00035577, ECO:0000256|HAMAP- CC Rule:MF_00920}; 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:0000256|HAMAP- CC Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00920}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00920}. Cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_00920}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. 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). {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 --------------------------------------------------------------------------- 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; AAGLQK010000001; EBP4056412.1; -; Genomic_DNA. DR EMBL; CP074675; QWI80807.1; -; Genomic_DNA. DR EMBL; CP077702; QXR63995.1; -; Genomic_DNA. DR RefSeq; WP_001528170.1; NZ_CP077702.1. DR AlphaFoldDB; A0A3T4RMW8; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; cd17874; FtsY; 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 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 NCBIfam; TIGR00064; ftsY; 1. DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1. DR PANTHER; PTHR43134:SF1; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 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; Domain of the SRP/SRP receptor G-proteins; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00920}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00920}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00920}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00920}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|HAMAP-Rule:MF_00920}. FT DOMAIN 461..474 FT /note="SRP54-type proteins GTP-binding" FT /evidence="ECO:0000259|PROSITE:PS00300" FT REGION 1..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 70..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..33 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 294..301 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT BINDING 376..380 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT BINDING 440..443 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" 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 //