ID A0A248YK43_9ACTN Unreviewed; 521 AA.
AC A0A248YK43;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CIK06_07130 {ECO:0000313|EMBL:ASW54005.1};
OS Plantactinospora sp. KBS50.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Plantactinospora.
OX NCBI_TaxID=2024580 {ECO:0000313|EMBL:ASW54005.1, ECO:0000313|Proteomes:UP000216795};
RN [1] {ECO:0000313|EMBL:ASW54005.1, ECO:0000313|Proteomes:UP000216795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS50 {ECO:0000313|EMBL:ASW54005.1,
RC ECO:0000313|Proteomes:UP000216795};
RA Juboi H., Hwang S.S., Yeo T.C., Nissom P.M.;
RT "Genome sequencing and analysis of secondary metabolite biosynthetic
RT capabilities of Plantactinospora sp. KBS50.";
RL Submitted (AUG-2017) 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; CP022961; ASW54005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248YK43; -.
DR KEGG; plk:CIK06_07130; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000216795; 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:UP000216795};
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 271..284
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
FT REGION 432..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
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 192..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
FT BINDING 250..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00306"
SQ SEQUENCE 521 AA; 55432 MW; F204CA4ACB327F6F CRC64;
MFDTLSDRLS GIFTKLRGKG RLTDADIDAT AREIRLALLE ADVALPVVKG FIGRIKERAR
GAEVSQALNP AQQVIKIVHE ELVAVLGGES RRLQFAKQPP TVIMLAGLQG SGKTTLAGKL
ARWLKAQGHQ PLLVAADLQR PNAVGQLQVL GGRAEVEVYA PEPGNGVGDP VRVARDSIEH
ARRAARDVVI VDTAGRLGID AEMMAQAANI RDAVDPDEVI FVIDAMVGQD AVRTAEAFRD
GVGISGVVLS KLDGDARGGA ALSVREVTGQ PILFASTGEK LEDFDVFHPD RMASRILGMG
DVLTLIEQAE QAFDADQKEK MTAKLMGGES FTLEDFLDQL IAVRRMGPIA NVLSMMPGMG
QMKDQLAELD DKHFDRVTAI IRSMTPGERS NPKIINGSRR ARIAGGSGVT VMDVNQLLNR
FADAQKMMKQ MGGMMGMPGG GRRKATKSPK NKRKGNKGGG RPRSGVGAGG GMPAGFPGGV
PQLPPGLDPN DLAGGGLPPG FKLPNLDFNK LGKGKRDDRR G
//
