ID A0A3M0BIU0_9AQUI Unreviewed; 304 AA. AC A0A3M0BIU0; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 02-OCT-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 ORFNames=CLV39_0968 {ECO:0000313|EMBL:RMA97310.1}; OS Hydrogenothermus marinus. OC Bacteria; Aquificota; Aquificia; Aquificales; Hydrogenothermaceae; OC Hydrogenothermus. OX NCBI_TaxID=133270 {ECO:0000313|EMBL:RMA97310.1, ECO:0000313|Proteomes:UP000280842}; RN [1] {ECO:0000313|EMBL:RMA97310.1, ECO:0000313|Proteomes:UP000280842} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VM1 {ECO:0000313|EMBL:RMA97310.1, RC ECO:0000313|Proteomes:UP000280842}; RA Goeker M.; RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II RT (KMG-II): from individual species to whole genera."; RL Submitted (OCT-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). {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. {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 -!- 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 EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RMA97310.1}. 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; REFO01000011; RMA97310.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3M0BIU0; -. DR OrthoDB; 9804720at2; -. DR Proteomes; UP000280842; Unassembled WGS sequence. 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:SF7; CELL DIVISION PROTEIN FTSY HOMOLOG, CHLOROPLASTIC; 1. DR PANTHER; PTHR43134; 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|HAMAP-Rule:MF_00920}; KW 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000280842}. FT DOMAIN 277..290 FT /note="SRP54-type proteins GTP-binding" FT /evidence="ECO:0000259|PROSITE:PS00300" FT BINDING 110..117 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT BINDING 192..196 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT BINDING 256..259 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" SQ SEQUENCE 304 AA; 33255 MW; B32ACC4AA03214B0 CRC64; MFKSMFERIK KGLEKTKNQI SESLYAISFG KKIDESLFEE IEFALLKADV GIDATEEIVE FLRKESKKRK ITEGEQLKEL LKEKLIDILT PCSGQLNLLG EKPDVILFLG INGSGKTTTV GKLAALLKNE GKSVVLAAAD TFRAAAIDQL EVWANRVGAR IVKHQPGADP AAVVFDAVNS AKSRGDDIVL VDTAGRLHTK EHLMKELQKI KRTIQKFSPN QPCETLLVLD GTIGQNSIKQ AQVFKESTDV SGIVITKLDG TAKGGALIPI CQKLQIPIKF IGVGEDIEDL QPFDPKSFVE AIIG //