SRP54_ACIAM
ID SRP54_ACIAM Reviewed; 451 AA.
AC P70722;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE Short=SRP54 {ECO:0000255|HAMAP-Rule:MF_00306};
DE Flags: Fragment;
GN Name=srp54 {ECO:0000255|HAMAP-Rule:MF_00306}; Synonyms=ffh;
OS Acidianus ambivalens (Desulfurolobus ambivalens).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=2283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Lei 10 / DSM 3772 / JCM 9191;
RX PubMed=9914525; DOI=10.1046/j.1432-1327.1999.00065.x;
RA Moll R., Schaefer G., Schmidtke S.;
RT "Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus
RT ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.";
RL Eur. J. Biochem. 259:441-448(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. {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; Y08735; CAA69991.1; -; Genomic_DNA.
DR PDB; 1J8M; X-ray; 2.00 A; F=1-292.
DR PDB; 1J8Y; X-ray; 2.00 A; F=1-292.
DR PDBsum; 1J8M; -.
DR PDBsum; 1J8Y; -.
DR AlphaFoldDB; P70722; -.
DR SMR; P70722; -.
DR EvolutionaryTrace; P70722; -.
DR GO; GO:0048500; C:signal recognition particle; IEA:InterPro.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN <1..451
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101171"
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"
FT NON_TER 1
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 43..59
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:1J8M"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1J8M"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1J8M"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:1J8M"
SQ SEQUENCE 451 AA; 50381 MW; EAA6F2D901748CEA CRC64;
SKLLDNLRDA VRKFLTGSSS YDKAVEDFIK ELQKSLISAD VNVKLVFSLT NKIKERLKNE
KPPTYIERRE WFIKIVYDEL SNLFGGDKEP KVIPDKIPYV IMLVGVQGTG KTTTAGKLAY
FYKKKGFKVG LVGADVYRPA ALEQLQQLGQ QIGVPVYGEP GEKDAVGIAK RGVEKFLSEK
MEIIIVDTAG RHGYGEEAAL LEEMKNIYEA IKPDEVTLVI DASIGQKAYD LASKFNQASK
IGTIIITKMD GTAKGGGALS AVAATGATIK FIGTGEKIDE LEVFNPRRFV ARILGMGDIE
TILEKIKEVE NYDKMQKKME EVISGKGKLT LRDVYNQLIA LRKMGPLSKL FQLLPGIGML
GQIPEDQLKV GEEKMRKWLA IMNSMTYEEL DNPSIIDKSR MRRIALGSGT EIEDVKELIE
HYNLMQRTIK MLKRRKKDVE KLLGQFGGES T