ID A0A0A1SMM7_PAESO Unreviewed; 450 AA.
AC A0A0A1SMM7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:CEQ04624.1};
GN ORFNames=R28058_23421 {ECO:0000313|EMBL:CEQ04624.1}, UMC4404_20591
GN {ECO:0000313|EMBL:CEO34362.1};
OS Paeniclostridium sordellii (Clostridium sordellii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Paeniclostridium.
OX NCBI_TaxID=1505 {ECO:0000313|EMBL:CEQ04624.1, ECO:0000313|Proteomes:UP000049127};
RN [1] {ECO:0000313|EMBL:CEO34362.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UMC4404 {ECO:0000313|EMBL:CEO34362.1};
RA Aslett M.A., De Silva N.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000049127, ECO:0000313|Proteomes:UP000049685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R28058 {ECO:0000313|EMBL:CEQ04624.1,
RC ECO:0000313|Proteomes:UP000049127}, and UMC4404
RC {ECO:0000313|Proteomes:UP000049685};
RA Aslett A.Martin., De Silva Nishadi;
RL Submitted (JAN-2015) 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; CDNY01000014; CEO34362.1; -; Genomic_DNA.
DR EMBL; CEKZ01000014; CEQ04624.1; -; Genomic_DNA.
DR RefSeq; WP_021127820.1; NZ_WQMV01000017.1.
DR AlphaFoldDB; A0A0A1SMM7; -.
DR GeneID; 57936847; -.
DR KEGG; psor:RSJ16_14325; -.
DR PATRIC; fig|1505.7.peg.2554; -.
DR eggNOG; COG0541; Bacteria.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000049127; Unassembled WGS sequence.
DR Proteomes; UP000049685; 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: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 Coiled coil {ECO:0000256|SAM:Coils};
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};
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 COILED 316..343
FT /evidence="ECO:0000256|SAM:Coils"
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 450 AA; 49747 MW; 3FEB78A21ABB402E CRC64;
MIFEGLADKL QGALGKLKSK GKLTEKDVKE AMREVKLALL EADVNFKVVK DFVKKVQERA
VGQEVMESLT PAQHVIKIVN EELTSLMGDV QSKIMISPKP PTVIMMVGLQ GAGKTTTSGK
LGGYFKKQGK KPLLVACDIY RPAAIKQLQV VGEKLDIPVF SMGDKESPVN IAKAGYNHAL
KNNNDLVIID TAGRLHIDET LMDELKNIKS EIKPHEILLV VDSMTGQDAV NVAESFNEAL
GVDGVVLTKL DGDTRGGAAL SIRAVTQKPI KFIGMGEKLD DLEPFHPDRM ASRILGMGDI
LSLIEKAQEN IDLEKAKELE SKIKKQELDF EDFLEQMEQI QKMGPLNKVL EMIPGMGQVK
DQLGDIDMNN KEIVKTKAIV QSMTIEERRN PSILNASRKK RIARGSGTSV QDVNRLIKQF
GEMKKMMKMF TGTQKSMKKR GGFAGLPFFK
//
