ID A0A6M2ARW5_9FLAO Unreviewed; 442 AA. AC A0A6M2ARW5; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 29-SEP-2021, entry version 6. DE RecName: Full=Signal recognition particle protein {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:NGX83582.1}; GN ORFNames=G3A46_04600 {ECO:0000313|EMBL:NGX83582.1}; OS Aequorivita sp. KMM 9714. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Aequorivita. OX NCBI_TaxID=2707173 {ECO:0000313|EMBL:NGX83582.1, ECO:0000313|Proteomes:UP000474662}; RN [1] {ECO:0000313|EMBL:NGX83582.1, ECO:0000313|Proteomes:UP000474662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ch27 {ECO:0000313|EMBL:NGX83582.1, RC ECO:0000313|Proteomes:UP000474662}; RA Isaeva M.P., Chernysheva N.Y.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:NGX83582.1, ECO:0000313|Proteomes:UP000474662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ch27 {ECO:0000313|EMBL:NGX83582.1, RC ECO:0000313|Proteomes:UP000474662}; RA Romanenko L.A., Kurilenko V.; RT "Aequorivita submarina sp. nov., isolated from the Chukchi Sea bottom RT sediments."; 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 -!- 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 -!- 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:NGX83582.1}. 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; JAAGRO010000001; NGX83582.1; -; Genomic_DNA. DR Proteomes; UP000474662; Unassembled WGS sequence. DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule. DR GO; GO:0008312; F:7S RNA binding; 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; 1.10.260.30; -; 1. DR Gene3D; 1.20.120.140; -; 1. DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11564; PTHR11564; 1. DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 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; SSF47446; SSF47446; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00959; ffh; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00306}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00306}; 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 268..281 FT /note="SRP54" FT /evidence="ECO:0000259|PROSITE:PS00300" FT NP_BIND 106..113 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT NP_BIND 189..193 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT NP_BIND 247..250 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306" FT COILED 303..323 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 442 AA; 48247 MW; C93E7CAE22EDF7D0 CRC64; MFDNLSDKLD KALHVLKGHG SITEVNVAET LKEVRRALLD ADVNFKTAKE FTNTVKEKAL GQDVLTTLQP GQLMVKLVKD ELTELMGGET AGINLSGAPT VILMSGLQGS GKTTFSGKLA NFLKTKKTKK PLLVACDVYR PAAINQLHVV GDQIGVEVYS EPENKNPVQI AQNAIEHAKK NGFNVVIVDT AGRLAIDEAM MTEIANVHKA INPQETLFVV DAMTGQDAVN TAKAFNERLN FDGVVLTKLD GDTRGGAAIS IKSVVNKPIK FIGTGEKMDA IDVFHPERMA DRILGMGDVV SLVERAQEQF DEEEARKLQK KIAKNQFGFD DFLNQIQQVK KMGSMKDLVG MIPGAGKALK DVDIDDDAFK GIEAIIHSMT PTERSQPSVI NGSRKKRIAK GSGTSVQQVN QLLKQFDQMS KMMKMMQGGG GRKMMQAMSK MR //