SRP54_THEAQ
ID SRP54_THEAQ Reviewed; 430 AA.
AC O07347;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306};
GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306};
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Freymann D.M., Keenan R.J., Stroud R.M., Walter P.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-295, AND DOMAIN.
RX PubMed=9002524; DOI=10.1038/385361a0;
RA Freymann D.M., Keenan R.J., Stroud R.M., Walter P.;
RT "Structure of the conserved GTPase domain of the signal recognition
RT particle.";
RL Nature 385:361-364(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=9695947; DOI=10.1016/s0092-8674(00)81418-x;
RA Keenan R.J., Freymann D.M., Walter P., Stroud R.M.;
RT "Crystal structure of the signal sequence binding subunit of the signal
RT recognition particle.";
RL Cell 94:181-191(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-295, AND DOMAIN.
RX PubMed=10426959; DOI=10.1038/11572;
RA Freymann D.M., Keenan R.J., Stroud R.M., Walter P.;
RT "Functional changes in the structure of the SRP GTPase on binding GDP and
RT Mg2+GDP.";
RL Nat. Struct. Biol. 6:793-801(1999).
RN [5]
RP CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DOMAIN.
RX PubMed=14501130; DOI=10.1107/s0907444903016573;
RA Shepotinovskaya I.V., Focia P.J., Freymann D.M.;
RT "Crystallization of the GMPPCP complex of the NG domains of Thermus
RT aquaticus Ffh and FtsY.";
RL Acta Crystallogr. D 59:1834-1837(2003).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00306}.
CC -!- INTERACTION:
CC O07347; P83749: ftsY; NbExp=3; IntAct=EBI-1037906, EBI-1037899;
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 ECO:0000269|PubMed:10426959, ECO:0000269|PubMed:14501130,
CC ECO:0000269|PubMed:9002524}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
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DR EMBL; U82109; AAB58502.1; -; Genomic_DNA.
DR RefSeq; WP_003045728.1; NZ_LHCI01000106.1.
DR PDB; 1FFH; X-ray; 2.05 A; A=2-295.
DR PDB; 1JPJ; X-ray; 2.30 A; A=1-296.
DR PDB; 1JPN; X-ray; 1.90 A; A/B=1-296.
DR PDB; 1LS1; X-ray; 1.10 A; A=1-295.
DR PDB; 1NG1; X-ray; 2.03 A; A=1-294.
DR PDB; 1O87; X-ray; 2.10 A; A/B=2-297.
DR PDB; 1OKK; X-ray; 2.05 A; A=1-294.
DR PDB; 1RJ9; X-ray; 1.90 A; B=1-300.
DR PDB; 1RY1; EM; 12.00 A; U=1-296.
DR PDB; 2C03; X-ray; 1.24 A; A/B=2-297.
DR PDB; 2C04; X-ray; 1.15 A; A/B=2-297.
DR PDB; 2CNW; X-ray; 2.39 A; A/B/C=2-294.
DR PDB; 2FFH; X-ray; 3.20 A; A/B/C=1-425.
DR PDB; 2IY3; EM; 16.00 A; A=2-296.
DR PDB; 2J45; X-ray; 1.14 A; A/B=2-297.
DR PDB; 2J46; X-ray; 1.14 A; A/B=2-297.
DR PDB; 2J7P; X-ray; 1.97 A; A/B=2-294.
DR PDB; 2NG1; X-ray; 2.02 A; A=2-294.
DR PDB; 2XKV; EM; 13.50 A; A=1-294.
DR PDB; 3NG1; X-ray; 2.30 A; A/B=1-294.
DR PDB; 3ZN8; EM; 12.00 A; A=2-295.
DR PDBsum; 1FFH; -.
DR PDBsum; 1JPJ; -.
DR PDBsum; 1JPN; -.
DR PDBsum; 1LS1; -.
DR PDBsum; 1NG1; -.
DR PDBsum; 1O87; -.
DR PDBsum; 1OKK; -.
DR PDBsum; 1RJ9; -.
DR PDBsum; 1RY1; -.
DR PDBsum; 2C03; -.
DR PDBsum; 2C04; -.
DR PDBsum; 2CNW; -.
DR PDBsum; 2FFH; -.
DR PDBsum; 2IY3; -.
DR PDBsum; 2J45; -.
DR PDBsum; 2J46; -.
DR PDBsum; 2J7P; -.
DR PDBsum; 2NG1; -.
DR PDBsum; 2XKV; -.
DR PDBsum; 3NG1; -.
DR PDBsum; 3ZN8; -.
DR AlphaFoldDB; O07347; -.
DR SMR; O07347; -.
DR IntAct; O07347; 1.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR EvolutionaryTrace; O07347; -.
DR GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
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; IPR004780; SRP.
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 PANTHER; PTHR11564:SF7; PTHR11564:SF7; 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 TIGRFAMs; TIGR00959; ffh; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..430
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101170"
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 245..248
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1LS1"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1FFH"
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:1LS1"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1LS1"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1LS1"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:2J45"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2J45"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2J45"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:1LS1"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 322..334
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 382..392
FT /evidence="ECO:0007829|PDB:2FFH"
FT HELIX 396..415
FT /evidence="ECO:0007829|PDB:2FFH"
SQ SEQUENCE 430 AA; 47356 MW; 49F76AB5BC5D7D3F CRC64;
MFQQLSARLQ EAIGRLRGRG RITEEDLKAT LREIRRALMD ADVNLEVARD FVERVREEAL
GKQVLESLTP AEVILATVYE ALKEALGGEA RLPVLKDRNL WFLVGLQGSG KTTTAAKLAL
YYKGKGRRPL LVAADTQRPA AREQLRLLGE KVGVPVLEVM DGESPESIRR RVEEKARLEA
RDLILVDTAG RLQIDEPLMG ELARLKEVLG PDEVLLVLDA MTGQEALSVA RAFDEKVGVT
GLVLTKLDGD ARGGAALSAR HVTGKPIYFA GVSEKPEGLE PFYPERLAGR ILGMGDVASL
AEKVRAAGLE AEAPKSAKEL SLEDFLKQMQ NLKRLGPFSE ILGLLPGVPQ GLKVDEKAIK
RLEAIVLSMT PEERKDPRIL NGSRRKRIAK GSGTSVQEVN RFIKAFEEMK ALMKSLEKKK
GRGLMGMFRR
