ID A0A432G6L2_9DELT Unreviewed; 423 AA. AC A0A432G6L2; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 11-DEC-2019, entry version 4. 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 ORFNames=DSY98_05900 {ECO:0000313|EMBL:RTZ79392.1}; OS SAR324 cluster bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria; SAR324 cluster. OX NCBI_TaxID=2024889 {ECO:0000313|EMBL:RTZ79392.1, ECO:0000313|Proteomes:UP000286732}; RN [1] {ECO:0000313|EMBL:RTZ79392.1, ECO:0000313|Proteomes:UP000286732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAG 63_2 {ECO:0000313|EMBL:RTZ79392.1}; RA Trembath-Reichert E., Huber J.A.; RT "Combined omics and stable isotope probing to characterize newly discovered RT Mariana Back-Arc vent microbial communities."; RL Submitted (JUN-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 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 -!- 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}. 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:RTZ79392.1}. 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; QNZM01000229; RTZ79392.1; -; Genomic_DNA. DR Proteomes; UP000286732; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule. 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; 1.20.120.140; -; 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, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Receptor {ECO:0000256|HAMAP-Rule:MF_00920}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..22 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 396..409 FT /note="SRP54" FT /evidence="ECO:0000259|PROSITE:PS00300" FT NP_BIND 229..236 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT NP_BIND 311..315 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT NP_BIND 375..378 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT COILED 47..96 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 423 AA; 47852 MW; 32184FF9967161D9 CRC64; MTTLILIGFA IFIILLCLFV WYRQHSRSLK SKAPEELSGR KKEKRLVQLE KEHAKTLELQ IKEEEKLREE KESAKLAKAE QREKELQEKI ASIEEERLHQ QVLQREIEKT AETVETPDEV DSFLERLRKG VIKTKTQLQD NLAEAVLGRK EINEDLLDDL EEVLIGSDIG PETTQRILDA ITEKVEREEL SSPQVLQSEI QLEIQKIMSK TYAVLGTTER KPLILLFVGV NGVGKTTTIG KIAAQYRQQG KKVLMGAGDT FRAAAIEQLV EWSRRADCDI IQKEPGGDPS AVMYETVQKG IDEDYDVVIC DTAGRLHTKK NLMEELKKMV RVIRKLIPDA PHEILLVLDA TTGQNAIFQT REFMEATDLT GLIITKLDGT SKGGVVIGIV NEFDIPVRYI GVGEQVEDLR PFDAQQFTES IFA //