ID A0A6G7ZAM0_9FIRM Unreviewed; 433 AA. AC A0A6G7ZAM0; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 02-OCT-2024, entry version 14. DE RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306}; DE EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00306}; DE AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306}; GN Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306, GN ECO:0000313|EMBL:QIK86009.1}; GN ORFNames=G7061_05075 {ECO:0000313|EMBL:QIK86009.1}; OS Erysipelothrix sp. HDW6B. OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Erysipelothrix. OX NCBI_TaxID=2714929 {ECO:0000313|EMBL:QIK86009.1, ECO:0000313|Proteomes:UP000503239}; RN [1] {ECO:0000313|EMBL:QIK86009.1, ECO:0000313|Proteomes:UP000503239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HDW6B {ECO:0000313|EMBL:QIK86009.1, RC ECO:0000313|Proteomes:UP000503239}; RA Hyun D.-W., Bae J.-W.; RT "Erysipelothrix sp. nov. isolated from aquatic animals."; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic signal CC sequence of the ribosome-nascent chain (RNC) as it emerges from the CC ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic CC membrane where it interacts with the SRP receptor FtsY. CC {ECO:0000256|HAMAP-Rule:MF_00306}. 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_00306}; 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_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which is CC responsible for interactions with the ribosome, the central G domain, CC which binds GTP, and the C-terminal M domain, which binds the RNA and CC the signal sequence of the RNC. {ECO:0000256|HAMAP-Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily. CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|HAMAP-Rule:MF_00306}. 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; CP049860; QIK86009.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G7ZAM0; -. DR Proteomes; UP000503239; Chromosome. DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule. DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro. 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 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 Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR004780; SRP. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR042101; SRP54_N_sf. DR NCBIfam; TIGR00959; ffh; 1. DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1. DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47446; Signal peptide-binding domain; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00306}; Reference proteome {ECO:0000313|Proteomes:UP000503239}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135, KW ECO:0000256|HAMAP-Rule:MF_00306}. FT DOMAIN 266..279 FT /note="SRP54-type proteins GTP-binding" FT /evidence="ECO:0000259|PROSITE:PS00300" FT BINDING 107..114 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT BINDING 187..191 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT BINDING 245..248 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" SQ SEQUENCE 433 AA; 47844 MW; 88B50029C33DD30B CRC64; MAFDNLTNRL QDTFKNLTGK GKLTEKNIAD ALSEIRISLL EADVSLEVIN ELLDYTRKEA MGMKVVRDVD PSQMFIKIVN DKLVEILGEE HQGLTFTRKP GVMMMVGLQG SGKTTSIAKI ARELKVKEDK KVLLVAADLA RPAAIEQLKI LGERIGVEVF AKENSTPVEV VTDALSYGKD FDVILIDTAG RLQIDEALMQ QLVDIQALAK PEEILLSVDA MSGQDVIHVA NGFKSKLNLT GLVATKFDGD SRGGSILSVR YMTKVPVKYV GVGEGIEELE AFHPDRTASR ILGMGDIVSL VEKAQEKMDI EASEKSAERM MNGQFTLDDM LIQLQQVSKM GPISGLLKML PGANQMANQI DDDDASKGMK KTEAMIQSMT KEERNDPTII RSGRKHRIAK GSGVTTTDVN RLLSQYDKMK KQMRMFSRMM GKQ //