SRP54_METJA
ID SRP54_METJA Reviewed; 451 AA.
AC Q57565;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=MJ0101;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98081.1; -; Genomic_DNA.
DR PIR; E64312; E64312.
DR RefSeq; WP_010869593.1; NC_000909.1.
DR PDB; 2V3C; X-ray; 2.50 A; C/D=3-427.
DR PDB; 3NDB; X-ray; 3.00 A; B=3-431.
DR PDB; 4XCO; X-ray; 2.90 A; C/D=304-451.
DR PDBsum; 2V3C; -.
DR PDBsum; 3NDB; -.
DR PDBsum; 4XCO; -.
DR AlphaFoldDB; Q57565; -.
DR SMR; Q57565; -.
DR DIP; DIP-46442N; -.
DR IntAct; Q57565; 1.
DR STRING; 243232.MJ_0101; -.
DR EnsemblBacteria; AAB98081; AAB98081; MJ_0101.
DR GeneID; 1450940; -.
DR KEGG; mja:MJ_0101; -.
DR eggNOG; arCOG01228; Archaea.
DR HOGENOM; CLU_009301_6_0_2; -.
DR InParanoid; Q57565; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 25871at2157; -.
DR PhylomeDB; Q57565; -.
DR EvolutionaryTrace; Q57565; -.
DR Proteomes; UP000000805; 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 DisProt; DP00897; -.
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..451
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101177"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 188..192
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 HELIX 4..15
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3NDB"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2V3C"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3NDB"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:2V3C"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:2V3C"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:3NDB"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:2V3C"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4XCO"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:4XCO"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:4XCO"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:3NDB"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:2V3C"
FT HELIX 407..423
FT /evidence="ECO:0007829|PDB:2V3C"
FT TURN 424..427
FT /evidence="ECO:0007829|PDB:3NDB"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:4XCO"
FT HELIX 437..445
FT /evidence="ECO:0007829|PDB:4XCO"
SQ SEQUENCE 451 AA; 50124 MW; 5EEAF505FD227914 CRC64;
MLDKLGENLN KALNKLKAAA FVDKKLIKEV IKDIQRALIQ ADVNVKLVLK MSKEIERRAL
EEKTPKGLSK KEHIIKIVYE ELVKLLGEEA KKLELNPKKQ NVILLVGIQG SGKTTTAAKL
ARYIQKRGLK PALIAADTYR PAAYEQLKQL AEKIHVPIYG DETRTKSPVD IVKEGMEKFK
KADVLIIDTA GRHKEEKGLL EEMKQIKEIT NPDEIILVID GTIGQQAGIQ AKAFKEAVGE
IGSIIVTKLD GSAKGGGALS AVAETKAPIK FIGIGEGIDD LEPFDPKKFI SRLLGMGDLE
SLLEKAEDMV DEKTEESIDA IMRGKFTLNE LMTQLEAIEN MGSMKKILSM IPGFGGAMPK
ELSHLTEAKI KKYKVIISSM TKEERENPKI IKASRIRRIA RGSGTTENDV REVLRYYETT
KNAIDKLRKG KMLRIGGPLG QIMRQLMFKE G
