ID   SRP54_AQUAE             Reviewed;         454 AA.
AC   O67615;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE   AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306};
GN   Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=aq_1720;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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:0000255|HAMAP-Rule:MF_00306}.
CC   -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC       system, which is composed of SRP and FtsY. {ECO:0000255|HAMAP-
CC       Rule:MF_00306}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}.
CC       Note=The SRP-RNC complex is targeted to the cytoplasmic membrane.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00306}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC       {ECO:0000255|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; AE000657; AAC07579.1; -; Genomic_DNA.
DR   PIR; E70448; E70448.
DR   RefSeq; NP_214181.1; NC_000918.1.
DR   RefSeq; WP_010881118.1; NC_000918.1.
DR   AlphaFoldDB; O67615; -.
DR   SMR; O67615; -.
DR   STRING; 224324.aq_1720; -.
DR   EnsemblBacteria; AAC07579; AAC07579; aq_1720.
DR   KEGG; aae:aq_1720; -.
DR   PATRIC; fig|224324.8.peg.1323; -.
DR   eggNOG; COG0541; Bacteria.
DR   HOGENOM; CLU_009301_6_0_0; -.
DR   InParanoid; O67615; -.
DR   OMA; DTAGRHK; -.
DR   OrthoDB; 656414at2; -.
DR   Proteomes; UP000000798; 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: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   Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT   CHAIN           1..454
FT                   /note="Signal recognition particle protein"
FT                   /id="PRO_0000101148"
FT   BINDING         102..109
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         184..188
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         242..245
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   454 AA;  50912 MW;  9F13FA8C883A0558 CRC64;
     MLELLTEKFS HALEKLTNAR KITEKNINQT LREIRLALLE ADVDYQVAKD FIKRIREKVV
     GKEVPKNLSP AEFVIKTVYE ELVDILGGEK ADLKKGTVLF VGLQGTGKTT TIGKIANLLK
     KGGHKVAVSS TDLRRPAAML QLQRLAERVG VPYYEFEEGL GAVEIARRAV KRAKEESVDY
     LLLDTAGRLH VDEELMKELQ EIKEVTNPSE ILYVADAMQG QTALETAKTF HERLGLTGVV
     ITKMDGDARG GLALSVKEVL GVPIKFIGVG EKIEDIEPFY PDRIAQRILG LGDIQSLVEK
     AQEVITEDKA QVMATKVMTG EFDLEDLREM LRMIQQMGPL DKLLSMIPGV APQLKHLKVD
     EKQFKKIEAI INSMTPEERR NPKIINMSRK KRIARGSGTT VSDVNKLLKR YEEMKKMMRK
     LQKAGGMPAI PKMPKMPRFP SEASSFNLFL FLST