SRP54_METKA
ID SRP54_METKA Reviewed; 447 AA.
AC Q8TUY9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=MK1612;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009439; AAM02825.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TUY9; -.
DR SMR; Q8TUY9; -.
DR STRING; 190192.MK1612; -.
DR EnsemblBacteria; AAM02825; AAM02825; MK1612.
DR KEGG; mka:MK1612; -.
DR PATRIC; fig|190192.8.peg.1775; -.
DR HOGENOM; CLU_009301_6_0_2; -.
DR OMA; DTAGRHK; -.
DR Proteomes; UP000001826; 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..447
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101178"
FT BINDING 108..115
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 246..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ SEQUENCE 447 AA; 49732 MW; EDE3844E1756D337 CRC64;
MIGFADRLAE ITKKIKGASI IDEDFVKEVV RDVQRALLEA DVDVKLVLEL SKRIEKRALE
EEPPAGVPKR DYLLRIVYEE LVELLGGEKT EGLDIDLSRD VNVIMLVGLY GMGKTTTAAK
LARYLQRKGY RVGLVGADPY RPAAGEQLRQ LAEEVDVPVH VEDVDDAVEM AVKGVEALKD
ECDVVIVDTA GRDRLSEDLI DELREMAERI EPHEVLLVLD ATVGQKAGDH AEAFHEAVQL
TGVVITKLDT AAKGGGALSA VARTGAPIKF VGTGERVDDL EEFNPRSFVA RLLGIGDIDE
LLRRTEEMLE EEEKAEDVLE GEFTLKDLYE QLEALSKMGP VDKLLQYVPG MGGGRNVRKI
SQITEERLKK YKVIMDSMTE KELENPEILN KSRIRRIAIG SGTSERDVIE LLNHYRMMKD
VIEDIQSGRI PRIGGELGRV IRNVLRG
