ID A0A1B1Y425_9FLAO Unreviewed; 448 AA.
AC A0A1B1Y425;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AXE80_04040 {ECO:0000313|EMBL:ANW95499.1};
OS Wenyingzhuangia fucanilytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Wenyingzhuangia.
OX NCBI_TaxID=1790137 {ECO:0000313|EMBL:ANW95499.1, ECO:0000313|Proteomes:UP000092967};
RN [1] {ECO:0000313|EMBL:ANW95499.1, ECO:0000313|Proteomes:UP000092967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ1127 {ECO:0000313|EMBL:ANW95499.1,
RC ECO:0000313|Proteomes:UP000092967};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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; CP014224; ANW95499.1; -; Genomic_DNA.
DR RefSeq; WP_068824685.1; NZ_CP014224.1.
DR AlphaFoldDB; A0A1B1Y425; -.
DR STRING; 1790137.AXE80_04040; -.
DR KEGG; wfu:AXE80_04040; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000092967; 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: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:UP000092967};
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 448 AA; 49005 MW; ECBDFE95A19D1F08 CRC64;
MFNNLSDKLD KALHVLKGHG KITEVNVAET LKEVRRALLD ADVNFKIAKE FTVRVKEKAL
GQNVLTTLNP GQLMVKLVKD ELAELMGGET AGVNLTGTPT VILMAGLQGS GKTTFSGKLA
NYLKTKKNKQ VLLVGADVYR PAAINQLQVV GEQIGIEVYA EVENKNPVEI AQNAIAHAKA
NGKNTVIIDT AGRLAIDEAL MTEISNIHKA VNPQETLFVV DSMTGQDAVN TAKAFNDLLN
FDGVVLTKLD GDTRGGAALT IKSVVNKPIK FIGTGEKMEA IDVFYPERMA DRILGMGDVV
SLVERAQEQY DEEEARKLQK KIAKDQFGFD DFLNQIQQIK KMGNMKDLVG MIPGAGKALK
DVDIDDDAFK GIEAIIKSMT PLERTEPKVI NASRKKRIAK GSGTSITEVN QLLKQFFQMS
KMMKMMQGGG SRKMMQMMQG MKGGMPRM
//