ID A0A432G6L2_9DELT Unreviewed; 423 AA. AC A0A432G6L2; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 27-NOV-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=DSY98_05900 {ECO:0000313|EMBL:RTZ79392.1}; OS SAR324 cluster bacterium. OC Bacteria; 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). {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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}. 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 AlphaFoldDB; A0A432G6L2; -. DR Proteomes; UP000286732; 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:0005047; F:signal recognition particle binding; IEA:TreeGrafter. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR CDD; cd17874; FtsY; 1. DR FunFam; 1.20.120.140:FF:000002; Signal recognition particle receptor FtsY; 1. DR FunFam; 3.40.50.300:FF:000053; Signal recognition particle receptor 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 Coiled coil {ECO:0000256|SAM:Coils}; 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, ECO:0000256|SAM:Phobius}; 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 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-type proteins GTP-binding" FT /evidence="ECO:0000259|PROSITE:PS00300" FT COILED 47..96 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 229..236 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT BINDING 311..315 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT BINDING 375..378 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" 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 //