ID G2Z314_FLABF Unreviewed; 449 AA.
AC G2Z314;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 ECO:0000313|EMBL:CCB70352.1};
GN OrderedLocusNames=FBFL15_2338 {ECO:0000313|EMBL:CCB70352.1};
OS Flavobacterium branchiophilum (strain FL-15).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB70352.1, ECO:0000313|Proteomes:UP000009186};
RN [1] {ECO:0000313|EMBL:CCB70352.1, ECO:0000313|Proteomes:UP000009186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB70352.1,
RC ECO:0000313|Proteomes:UP000009186};
RX PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG 1:IP;
RG Microbial Evolutionary Genomics,F-75015 Paris;
RG France 2:CNRS;
RG URA2171;
RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG INRA,78352 Jouy en Josas Cedex;
RG France. 4:Unite de Mathemathique;
RG Informatique et Genome,INRA;
RG 78352 Jouy en Josas Cedex;
RG France. 5:CEA/Genoscope;
RG Evry;
RG France;
RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA Rocha E.P., Duchaud E.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT branchiophilum.";
RL Appl. Environ. Microbiol. 77:7656-7662(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; FQ859183; CCB70352.1; -; Genomic_DNA.
DR RefSeq; WP_014084812.1; NC_016001.1.
DR AlphaFoldDB; G2Z314; -.
DR STRING; 1034807.FBFL15_2338; -.
DR KEGG; fbr:FBFL15_2338; -.
DR eggNOG; COG0541; Bacteria.
DR HOGENOM; CLU_009301_6_0_10; -.
DR Proteomes; UP000009186; 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:UP000009186};
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 268..281
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT BINDING 106..113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 189..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ SEQUENCE 449 AA; 49649 MW; 9E30298F230FB9FC CRC64;
MFSNLSEKLD KAFHVLKGHG KITEINVAET LKEVRRALLD ADVNFKIAKD FTTKVKDKAI
GQNVLTTLQP GQLLVKLVKD ELTELMGGDV AGINLSGNPS IILMSGLQGS GKTTFSGKLA
HYLKTKKHKK PLLVACDIYR PAAINQLHVV GKQIDVEVYS EIGNQNPVEI SQNAIKYAKE
KGFNVVIIDT AGRLAVDEEM MTEIANVHQA IKPNETLFVV DSMTGQDAVN TAKAFNDRLN
FDGVILTKLD GDTRGGAALS IKTVVNKPIK FIGTGEKMDA LDVFYPERMA ERILGMGDVV
SLVERAQEQF NEEEARKIQK KIAKNEFGFD DFLTQIQQVK KMGNMKDLIG MIPGASKAMK
DIEIEDDAFK HIEAIIHSMT PIERKKPAII DVKRKTRIAK GSGRKIEEVN QLMKQFDQMS
KMMKMMQGPG GKNLMKMMGN MKGGGAMPR
//
