ID   SRP54_SULIL             Reviewed;         447 AA.
AC   C3MPN4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=LS215_1339;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP35347.1; -; Genomic_DNA.
DR   RefSeq; WP_012713654.1; NC_012589.1.
DR   AlphaFoldDB; C3MPN4; -.
DR   SMR; C3MPN4; -.
DR   EnsemblBacteria; ACP35347; ACP35347; LS215_1339.
DR   GeneID; 7797855; -.
DR   KEGG; sis:LS215_1339; -.
DR   HOGENOM; CLU_009301_6_0_2; -.
DR   OMA; DTAGRHK; -.
DR   OrthoDB; 25871at2157; -.
DR   Proteomes; UP000001747; 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..447
FT                   /note="Signal recognition particle 54 kDa protein"
FT                   /id="PRO_1000205013"
FT   BINDING         103..110
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         185..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         245..248
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   447 AA;  49952 MW;  7B7281304E9BA73F CRC64;
     MLENIRDAVR KFLTGSTPYE KAVDEFIKEL QKSLISSDVN VKLVFSLTAK IKERLNKEKP
     PSVLERKEWF ISIVYDELSK LFGGDKEPNV NPTRLPFIIM LVGVQGSGKT TTAGKLAYFY
     KRRGYKVGLV AADVYRPAAY DQLLQLGNQI GVPVYGEPNN QNAIEIAKKG VDTFVKNKMD
     IIIVDTAGRH GYGEETKLLE EMKEIYEALK PDDVILVIDA SIGQKAYDLA SRFHQASPIG
     SIIITKMDGT AKGGGALSAV AATGATIKFI GTGEKIDELE IFNAKRYVSR ILGMGDIESI
     LEKVKGLEEY EKIQKKMEDV MEGKGKLTLR DVYAQIMALR KMGPLSKVLQ HIPGLGVMLP
     TPSEDQLKLG EEKIRRWLAA LNSMTYKELE NPSIIDKSRM RRIAEGSGLE VEDVRELLEW
     YNNMNKLLKM VKRRRGSIDK LFGGKIG