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Database: UniProt
Entry: A0A0S2W401_9FIRM
LinkDB: A0A0S2W401_9FIRM
Original site: A0A0S2W401_9FIRM 
ID   A0A0S2W401_9FIRM        Unreviewed;       452 AA.
AC   A0A0S2W401;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Signal recognition particle protein {ECO:0000256|HAMAP-Rule:MF_00306};
DE            EC=3.6.5.4 {ECO:0000256|HAMAP-Rule:MF_00306};
DE   AltName: Full=Fifty-four homolog {ECO:0000256|HAMAP-Rule:MF_00306};
GN   Name=ffh {ECO:0000256|HAMAP-Rule:MF_00306};
GN   ORFNames=C7373_102291 {ECO:0000313|EMBL:PVY59307.1}, IB211_01486c
GN   {ECO:0000313|EMBL:ALP93879.1};
OS   Intestinimonas butyriciproducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX   NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP93879.1, ECO:0000313|Proteomes:UP000064844};
RN   [1] {ECO:0000313|EMBL:ALP93879.1, ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|EMBL:ALP93879.1,
RC   ECO:0000313|Proteomes:UP000064844};
RX   PubMed=26620920; DOI=10.1038/ncomms10062;
RA   Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT   "Production of butyrate from lysine and the Amadori product fructoselysine
RT   by a human gut commensal.";
RL   Nat. Commun. 6:10062-10062(2015).
RN   [2] {ECO:0000313|Proteomes:UP000064844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA   de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT   "A butyrogenic pathway from the amino acid lysine in a human gut
RT   commensal.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PVY59307.1, ECO:0000313|Proteomes:UP000245778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26588 {ECO:0000313|EMBL:PVY59307.1,
RC   ECO:0000313|Proteomes:UP000245778};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00306}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00035577, ECO:0000256|HAMAP-
CC         Rule:MF_00306};
CC   -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC       system, which is composed of SRP and FtsY. {ECO:0000256|HAMAP-
CC       Rule:MF_00306}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306}.
CC       Note=The SRP-RNC complex is targeted to the cytoplasmic membrane.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00306}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|HAMAP-Rule:MF_00306}.
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DR   EMBL; CP011307; ALP93879.1; -; Genomic_DNA.
DR   EMBL; QEKK01000002; PVY59307.1; -; Genomic_DNA.
DR   RefSeq; WP_058117617.1; NZ_QEKK01000002.1.
DR   AlphaFoldDB; A0A0S2W401; -.
DR   STRING; 1297617.IB211_01486c; -.
DR   GeneID; 60290942; -.
DR   KEGG; ibu:IB211_01486c; -.
DR   PATRIC; fig|1297617.4.peg.1527; -.
DR   eggNOG; COG0541; Bacteria.
DR   OrthoDB; 9804720at2; -.
DR   Proteomes; UP000064844; Chromosome.
DR   Proteomes; UP000245778; Unassembled WGS sequence.
DR   GO; GO:0048500; C:signal recognition particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd18539; SRP_G; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR   Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 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; IPR004780; SRP.
DR   InterPro; IPR022941; SRP54.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   NCBIfam; TIGR00959; ffh; 1.
DR   PANTHER; PTHR11564:SF7; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00306};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00306};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00306};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00306}; Reference proteome {ECO:0000313|Proteomes:UP000064844};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00306};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00306};
KW   Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW   ECO:0000256|HAMAP-Rule:MF_00306}.
FT   DOMAIN          269..282
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   BINDING         108..115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         190..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT   BINDING         248..251
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   452 AA;  48968 MW;  3DF5481566B2F9CE CRC64;
     MAFEGLTEKL SNAFKKLRGK GRLSEADVKE AMREIRLALL EADVSFKVVK DFIARVTERA
     VGADVLESLT PAQMIVKIVN EELTALMGGD SVKLNLSSRP PTVVMVVGLN GAGKTTNCAK
     LAGFMKKQNG KRPLLAACDT FRPAAIHQLE VVGEQLGIPV FQMGQSDPVD IAKSAIEHAK
     KHGNDLVFLD TAGRLHVDEE LMEQLKVMKA AVDPDEILLV VDAMIGQDAV NAAKAFDEAL
     DITGVMLTKL DGDARGGAAL SIKAVTGKPI KFVGVGEKLD QVEVFHPDRM SSRILGMGDV
     LSLIEKAQQN FDLKKAAELQ EKMKKNRLTL TDFYDQLVQF KGMGSMQDLA GMLPGVDAKA
     LEGADLDKNA LGKTEAIILS MTPEERENPA LLNSSRKKRI AAGSGTQVVD VNRLLKQFEM
     MQQMTRQMAG MSGGKMARKM ARLGKMKGGF PF
//
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