SRP54_SACS2
ID SRP54_SACS2 Reviewed; 447 AA.
AC Q97ZE7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=SSO0971;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK41245.1; -; Genomic_DNA.
DR PIR; F90248; F90248.
DR RefSeq; WP_010923154.1; NC_002754.1.
DR PDB; 1QZW; X-ray; 4.10 A; A/C/E/G=1-432.
DR PDB; 1QZX; X-ray; 4.00 A; A/B=1-432.
DR PDB; 2IY3; EM; 16.00 A; A=297-432.
DR PDB; 3KL4; X-ray; 3.50 A; A=2-432.
DR PDB; 3ZN8; EM; 12.00 A; M=308-431.
DR PDB; 5L3S; X-ray; 1.90 A; A/C/E/G=1-292.
DR PDB; 5L3V; X-ray; 2.30 A; A/B=1-293.
DR PDBsum; 1QZW; -.
DR PDBsum; 1QZX; -.
DR PDBsum; 2IY3; -.
DR PDBsum; 3KL4; -.
DR PDBsum; 3ZN8; -.
DR PDBsum; 5L3S; -.
DR PDBsum; 5L3V; -.
DR AlphaFoldDB; Q97ZE7; -.
DR SMR; Q97ZE7; -.
DR STRING; 273057.SSO0971; -.
DR EnsemblBacteria; AAK41245; AAK41245; SSO0971.
DR GeneID; 27427290; -.
DR KEGG; sso:SSO0971; -.
DR PATRIC; fig|273057.12.peg.970; -.
DR eggNOG; arCOG01228; Archaea.
DR HOGENOM; CLU_009301_6_0_2; -.
DR InParanoid; Q97ZE7; -.
DR OMA; DTAGRHK; -.
DR PhylomeDB; Q97ZE7; -.
DR EvolutionaryTrace; Q97ZE7; -.
DR Proteomes; UP000001974; 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 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..447
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101187"
FT BINDING 103..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 185..189
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 5..13
FT /evidence="ECO:0007829|PDB:5L3V"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3KL4"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5L3S"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:5L3S"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:3KL4"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:3KL4"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:3KL4"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:3KL4"
FT HELIX 411..429
FT /evidence="ECO:0007829|PDB:3KL4"
SQ SEQUENCE 447 AA; 50047 MW; 2A21A42E9E4ED9E2 CRC64;
MLENIRDAVR KFLTGSTPYE KAVDEFIKDL QKSLISSDVN VKLVFSLTAK IKERLNKEKP
PSVLERKEWF ISIVYDELSK LFGGDKEPNV NPTKLPFIIM LVGVQGSGKT TTAGKLAYFY
KKRGYKVGLV AADVYRPAAY DQLLQLGNQI GVQVYGEPNN QNPIEIAKKG VDIFVKNKMD
IIIVDTAGRH GYGEETKLLE EMKEMYDVLK PDDVILVIDA SIGQKAYDLA SRFHQASPIG
SVIITKMDGT AKGGGALSAV VATGATIKFI GTGEKIDELE TFNAKRFVSR ILGMGDIESI
LEKVKGLEEY DKIQKKMEDV MEGKGKLTLR DVYAQIIALR KMGPLSKVLQ HIPGLGIMLP
TPSEDQLKIG EEKIRRWLAA LNSMTYKELE NPNIIDKSRM RRIAEGSGLE VEEVRELLEW
YNNMNRLLKM VKRRRGNIDK LFGGKIG
