SRP54_AERPE
ID SRP54_AERPE Reviewed; 441 AA.
AC Q9YB62;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=APE_1735;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(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; BA000002; BAA80736.1; -; Genomic_DNA.
DR PIR; C72556; C72556.
DR PDB; 7EPK; X-ray; 2.70 A; A=1-441.
DR PDBsum; 7EPK; -.
DR AlphaFoldDB; Q9YB62; -.
DR SMR; Q9YB62; -.
DR STRING; 272557.APE_1735; -.
DR EnsemblBacteria; BAA80736; BAA80736; APE_1735.
DR KEGG; ape:APE_1735; -.
DR PATRIC; fig|272557.25.peg.1168; -.
DR eggNOG; arCOG01228; Archaea.
DR OMA; DTAGRHK; -.
DR Proteomes; UP000002518; 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; 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; 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..441
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101172"
FT BINDING 103..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 184..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 244..247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7EPK"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:7EPK"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 255..262
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 293..320
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:7EPK"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:7EPK"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:7EPK"
SQ SEQUENCE 441 AA; 49114 MW; DDF8FA9BA7B999BE CRC64;
MMEGVRRAVA KFLRGGGVYE KAVDAFVKDL QRELIKADVN VKLVLNVTRR IKERALKEEP
PPGVTRRDWM IKIVYEELVK LFGGDQEPQV DPPKTPWIVL LVGVQGSGKT TTAGKLAYYY
VRRGYKVGLV SSDTHRPGAY EQLKRLAEEA GAMFYGEREG DPAEIARRGL EDLLSRGAEI
VIVDTAGRHG HGEEARLLDE MKAIASKVRP DEVALVIDAS IGQKAMGLAE RFHKSTPIGS
IIVTKMDGTA RGGGALTAAA VTGARIKFIG TGETLGELEP FAPRRFVARI LGMGDLESLL
ERIKSLEEAG ELDRAAEDVL KGRITMRTIY RQLRAMRKLG PLGKVLQMLP GASMLASIDE
GALKLGEEKM KRWMAIIESM TYEELDRPEI IDKRRMRRIA IGSGTSVDDV RELLVYYKNL
KTMMKKLKRD KRLLRRLGME L
