ID   SRP54_HALS3             Reviewed;         460 AA.
AC   B0R7X3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=OE_4450R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP14842.1; -; Genomic_DNA.
DR   RefSeq; WP_010903838.1; NC_010364.1.
DR   AlphaFoldDB; B0R7X3; -.
DR   SMR; B0R7X3; -.
DR   EnsemblBacteria; CAP14842; CAP14842; OE_4450R.
DR   GeneID; 5953980; -.
DR   GeneID; 62885589; -.
DR   KEGG; hsl:OE_4450R; -.
DR   HOGENOM; CLU_009301_6_0_2; -.
DR   OMA; DTAGRHK; -.
DR   PhylomeDB; B0R7X3; -.
DR   Proteomes; UP000001321; 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..460
FT                   /note="Signal recognition particle 54 kDa protein"
FT                   /id="PRO_1000115619"
FT   BINDING         104..111
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   460 AA;  50149 MW;  8361B782E651352E CRC64;
     MVLDDLGSSL RGTLDTLRGK SRISEEDVDK VVKEIQRSLL QADVDVDLVM DLSESITERS
     LEEEPPGGTS ARDHVLRIVY EELVGLVGDS TPIPLEEQTI MLAGLQGSGK TTTAAKMAWW
     FSKKGLRPAI VQTDTFRPGA YEQAAEMADR AEVDFYGEPD SDDPVQIARD GLAATADADV
     HIVDTAGRHA LEDDLIAEIE EIEGVVEPDR SLLVLDAAIG QGAKQQARQF DASIGIDGVA
     ITKLDGTAKG GGSLTAVNET DSTIAFLGSG ETVQDIERFE PDSFISRLLG MGDLKQLTER
     VERAMEETQD DDEDWDPEDL MKGEFTLHDM RKQMQAMDNM GPLDQVMDMI PGMGGGLMDE
     LPDDAMDVTQ ERMRGFEVIM DSMTEAEMAD PRSVGASQIR RIARGSGQPE DRVRELLDQH
     KMMAQTMQQF QGMGDGDMQR MMSKMQQQGG GGGGGFGGMF