SRP54_PYRFU
ID SRP54_PYRFU Reviewed; 443 AA.
AC Q8U070; Q977Q0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=PF1731;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH RNA.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11696367; DOI=10.1016/s0014-5793(01)02996-9;
RA Maeshima H., Okuno E., Aimi T., Morinaga T., Itoh T.;
RT "An archaeal protein homologous to mammalian SRP54 and bacterial Ffh
RT recognizes a highly conserved region of SRP RNA.";
RL FEBS Lett. 507:336-340(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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 (Probable). {ECO:0000305}.
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; AB057373; BAB64926.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81855.1; -; Genomic_DNA.
DR RefSeq; WP_011012877.1; NZ_CP023154.1.
DR PDB; 3DM5; X-ray; 2.51 A; A/B=1-443.
DR PDBsum; 3DM5; -.
DR AlphaFoldDB; Q8U070; -.
DR SMR; Q8U070; -.
DR STRING; 186497.PF1731; -.
DR TCDB; 3.A.5.7.2; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAL81855; AAL81855; PF1731.
DR GeneID; 41713562; -.
DR KEGG; pfu:PF1731; -.
DR PATRIC; fig|186497.12.peg.1799; -.
DR eggNOG; arCOG01228; Archaea.
DR HOGENOM; CLU_009301_6_0_2; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 25871at2157; -.
DR PhylomeDB; Q8U070; -.
DR BRENDA; 3.6.5.4; 5243.
DR EvolutionaryTrace; Q8U070; -.
DR Proteomes; UP000001013; 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.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..443
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101183"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 189..193
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"
FT CONFLICT 150
FT /note="L -> V (in Ref. 1; BAB64926)"
FT /evidence="ECO:0000305"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:3DM5"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3DM5"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:3DM5"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:3DM5"
FT HELIX 409..427
FT /evidence="ECO:0007829|PDB:3DM5"
SQ SEQUENCE 443 AA; 49879 MW; 102D1717B207F71A CRC64;
MVLDNLGKAL ANTLKKIARA SSVDEALIKE LVRDIQRALI QADVNVRLVL QLTREIQRRA
LEEKPPAGIS KKEHIIKIVY EELTKFLGTE AKPIEIKEKP TILLMVGIQG SGKTTTVAKL
ARYFQKRGYK VGVVCSDTWR PGAYHQLRQL LDRYHIEVFG NPQEKDAIKL AKEGVDYFKS
KGVDIIIVDT AGRHKEDKAL IEEMKQISNV IHPHEVILVI DGTIGQQAYN QALAFKEATP
IGSIIVTKLD GSAKGGGALS AVAATGAPIK FIGTGEKIDD IEPFDPPRFV SRLLGLGDIQ
GLLEKFKELE KEVEIKEEDI ERFLRGKFTL KDMYAQLEAM RKMGPLKQIL RMIPGLGYSL
PDDVISIGEE RLKKFKVIMD SMTEEELLNP EIINYSRIKR IARGSGTSTK DVKELLDQYR
QMKKLFKSMN KRQLSRLARR FGM
