ID   SRP54_HYPBU             Reviewed;         447 AA.
AC   A2BNB5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Hbut_1662;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM81476.1; -; Genomic_DNA.
DR   RefSeq; WP_011822794.1; NC_008818.1.
DR   AlphaFoldDB; A2BNB5; -.
DR   SMR; A2BNB5; -.
DR   STRING; 415426.Hbut_1662; -.
DR   EnsemblBacteria; ABM81476; ABM81476; Hbut_1662.
DR   GeneID; 4782384; -.
DR   KEGG; hbu:Hbut_1662; -.
DR   eggNOG; arCOG01228; Archaea.
DR   HOGENOM; CLU_009301_6_0_2; -.
DR   OMA; DTAGRHK; -.
DR   OrthoDB; 25871at2157; -.
DR   Proteomes; UP000002593; 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; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT   CHAIN           1..447
FT                   /note="Signal recognition particle 54 kDa protein"
FT                   /id="PRO_0000322242"
FT   BINDING         105..112
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         187..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   BINDING         247..250
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   447 AA;  50216 MW;  A773826528535DB3 CRC64;
     MPGLDDIRRA VSKLLKRSGP YENIVNEFIR DLQRALISAD VNVRLVFNLT KRIRERALKE
     QPPPGLSRRE WLVKLTYDEL VKLFGGEYEP EVKPPYTPYV IMMVGVQGSG KTTTVGKLAK
     FYRGMGYRVG VVAADTYRPG AYEQLKQLAD RAGAMFYGEP GSKDPVGIAR RGVEELKQRG
     ADIVIVDTAG RHGYGEEEAL LDEMKRIAEA IKPDEVVLVI DAAMGQKSYD LAKRFHEATP
     VGSIIVTKMD GTAKGGGALS AVAATGARIK FIGTGEDIDE IEVFRPKRFV ARLLGMGDLE
     SLLEKIERLR GVEEFEKTVA EMMSGKITFR TIYKQLQQVT KLGPFRKILQ MIPGISTMLE
     SLDEAARLSE EKVKKWLTIM NSMTYEELDN PNLLEERSRV KRIAVGAGVE PSEVRELYNY
     YKSVKKMMRQ LKKRKDLLER FARLGGV