ID   SRP54_PYRIL             Reviewed;         433 AA.
AC   A1RS43;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE            Short=SRP54 {ECO:0000255|HAMAP-Rule:MF_00306};
GN   Name=srp54 {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=Pisl_0597;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) 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:0000255|HAMAP-Rule:MF_00306}.
CC   -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC       system, which is composed of SRP and FtsY. Archaeal SRP consists of a
CC       7S RNA molecule of 300 nucleotides and two protein subunits: SRP54 and
CC       SRP19. {ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000504; ABL87775.1; -; Genomic_DNA.
DR   RefSeq; WP_011762351.1; NC_008701.1.
DR   AlphaFoldDB; A1RS43; -.
DR   SMR; A1RS43; -.
DR   STRING; 384616.Pisl_0597; -.
DR   EnsemblBacteria; ABL87775; ABL87775; Pisl_0597.
DR   GeneID; 4617621; -.
DR   KEGG; pis:Pisl_0597; -.
DR   eggNOG; arCOG01228; Archaea.
DR   HOGENOM; CLU_009301_6_0_2; -.
DR   OMA; DTAGRHK; -.
DR   OrthoDB; 25871at2157; -.
DR   Proteomes; UP000002595; Chromosome.
DR   GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0008312; F:7S RNA binding; 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; 1.10.260.30; -; 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; IPR036225; SRP/SRP_N.
DR   InterPro; IPR022941; SRP54.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   PANTHER; PTHR11564; PTHR11564; 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; SSF47364; SSF47364; 1.
DR   SUPFAM; SSF47446; SSF47446; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   CHAIN           1..433
FT                   /note="Signal recognition particle 54 kDa protein"
FT                   /id="PRO_0000300760"
FT   BINDING         106..113
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         186..190
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         244..247
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   433 AA;  48337 MW;  BF2C267D07277C3C CRC64;
     MKALGEVFSK LVEKIRGVSY IDEATLQELS REIQRALLKA DVPLDMVKTF TENAVKRMRE
     EKPPAGIPPR EYVLYILYDE LVKLLGGEQP AEFKPVKKPY LVLLLGVEGS GKTTTAAKLA
     RYLVKRGYRV GLVETDTIRP AAFDQLKQLA EKIGVPFYGE RDSKDAVEIA RRGVQNFKNM
     DVVIIDTAGR HKNEEALLQE VKMIYEAVNP DEVILVIDAT VGKLAAAQAE AFMKYLPIHS
     VIITKMDSTA RGGGALAAVI KTGARVKFIG VGEDVDEFDL FNPRKFVARV LGMGDLDALV
     EKIKAVFEEE KVLQEIESGR LDLLTFKKQI EGLLKLGPLS KVLQLLPGGF AAKISEEQVE
     LSQKNLKKWY AILSSMTIEE LKNPDILNAS RIRRIALGAG VTPKDVKEML TVYENLKKMS
     KTLKRQLRMR IPK