SRP54_ARCFU
ID SRP54_ARCFU Reviewed; 433 AA.
AC O29633;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=AF_0622;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10684931; DOI=10.1093/nar/28.6.1365;
RA Bhuiyan S.H., Gowda K., Hotokezaka H., Zwieb C.;
RT "Assembly of archaeal signal recognition particle from recombinant
RT components.";
RL Nucleic Acids Res. 28:1365-1373(2000).
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 (Probable).
CC {ECO:0000305|PubMed:10684931}.
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, ECO:0000269|PubMed:10684931}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306,
CC ECO:0000269|PubMed:10684931}. Note=The SRP-RNC complex is targeted to
CC the cytoplasmic membrane. {ECO:0000305}.
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; AE000782; AAB90619.1; -; Genomic_DNA.
DR PIR; F69327; F69327.
DR RefSeq; WP_010878126.1; NC_000917.1.
DR PDB; 2JQE; NMR; -; A=313-425.
DR PDBsum; 2JQE; -.
DR AlphaFoldDB; O29633; -.
DR BMRB; O29633; -.
DR SMR; O29633; -.
DR STRING; 224325.AF_0622; -.
DR PRIDE; O29633; -.
DR EnsemblBacteria; AAB90619; AAB90619; AF_0622.
DR GeneID; 24794225; -.
DR KEGG; afu:AF_0622; -.
DR eggNOG; arCOG01228; Archaea.
DR HOGENOM; CLU_009301_6_0_2; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 25871at2157; -.
DR PhylomeDB; O29633; -.
DR EvolutionaryTrace; O29633; -.
DR Proteomes; UP000002199; 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.
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..433
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101173"
FT BINDING 100..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 180..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 238..241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:2JQE"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:2JQE"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:2JQE"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2JQE"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2JQE"
FT HELIX 398..414
FT /evidence="ECO:0007829|PDB:2JQE"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:2JQE"
SQ SEQUENCE 433 AA; 48228 MW; 85FB475F846F4F72 CRC64;
MALESLKEVA RKIAGSSSID KKFVEEMVKE IQRALIKADV NVRQVKEISD AIKKRALSED
VLPALNAKEQ ILKIVYEELL RGVGEGLEIP LKKAKIMLVG LQGSGKTTTT AKMAKYFKDR
GMKVAVVAAD TWRPAAYEQL RQLAEEYGIT FYGEKGEKDA VKIVKNALEK LKDHDMIIID
TAGRHALEDE LIDEMIKIAE VARPDYKLLV LDAAIGQLAS KQAQAFHEAI GINGIIITKF
DGTAKGGGAL SAARQIGIPI AFIGTGEKVE DFERFDPAGF VSRLLGMGDI KALMEKIERI
ASEEELDPEA FLKGTFTLKD IYKQIEAMNK MGPVRKIFEM LPFGLGLKVD NDVMEMTQEK
MKKFRVIMDS MTEEELLNPK IIDSSRIRRI AIGSGTSPQE VKELLNYYKT MKNLMKKMKK
NKLPIKGLGK LGF
