ID F6EIV0_HOYSD Unreviewed; 519 AA.
AC F6EIV0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=AS9A_1562 {ECO:0000313|EMBL:AEF40011.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF40011.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF40011.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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; CP002786; AEF40011.1; -; Genomic_DNA.
DR RefSeq; WP_013806360.1; NC_015564.1.
DR AlphaFoldDB; F6EIV0; -.
DR STRING; 443218.AS9A_1562; -.
DR KEGG; asd:AS9A_1562; -.
DR eggNOG; COG0541; Bacteria.
DR HOGENOM; CLU_009301_6_0_11; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000009235; Chromosome.
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:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 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:UP000009235};
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 282..295
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 444..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..467
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 203..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 261..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ SEQUENCE 519 AA; 54970 MW; C56B3D1482884ED8 CRC64;
MFDSLSDRLN GALKGLRGKG RLTDADIDAT CREIRLALLE ADVALPVVRE FIKQIKVRAK
GAEVHGALNP AQQVIKIVNE ELVGILGGET RRLSLAKNPP TVIMLAGLQG SGKTTLAGKL
AKYLKAQGHA PMLVACDLQR PGAVTQLQIV GEKAGVNVFA PHPGTSIGGG ANPLGITASD
PVNVARDGVA EARTKQYDVV IVDTAGRLGI DEELMEQAAN IRDAVQPDET LFVLDAMVGQ
DAVSTANAFA EGVGFTGVVL TKLDGDARGG AALSVREVTG RPIMFASTGE KLEDFDVFHP
DRMASRILGM GDLLSLIEQA EQVFDAQEAE ATAQKIGSGE LTLEDFLDQL MAIRKMGPIA
NLMGMLPGAG QMKDALDQVD EKQLDRIQAI IRGMTPAERA NPKIINASRR LRIANGSGVK
VSDVNQLVDR FFEARKMMSA MAGRMGLPGS QRRRTKKGKK GKGRGRGPTP PKVRGGMPGG
LPAGMPNLSG MPKGLDELPP GLEGLDLSQL NLPNQGKKK
//
