SRP54_BUCAI
ID SRP54_BUCAI Reviewed; 451 AA.
AC P57473; Q9L4J1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Signal recognition particle protein {ECO:0000255|HAMAP-Rule:MF_00306};
DE AltName: Full=Fifty-four homolog {ECO:0000255|HAMAP-Rule:MF_00306};
GN Name=ffh {ECO:0000255|HAMAP-Rule:MF_00306}; OrderedLocusNames=BU393;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10781569; DOI=10.1128/jb.182.10.2967-2969.2000;
RA Jimenez N., Gonzalez-Candelas F., Silva F.J.;
RT "Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays
RT changes in the regulatory domain that suggest its desensitization to
RT inhibition by phenylalanine.";
RL J. Bacteriol. 182:2967-2969(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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. Interaction
CC with FtsY leads to the transfer of the RNC complex to the Sec
CC translocase for insertion into the membrane, the hydrolysis of GTP by
CC both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into
CC the individual components. {ECO:0000255|HAMAP-Rule:MF_00306}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein
CC composed of Ffh and a 4.5S RNA molecule. {ECO:0000255|HAMAP-
CC Rule:MF_00306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}.
CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00306}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00306}.
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DR EMBL; AJ239043; CAB90997.1; -; Genomic_DNA.
DR EMBL; BA000003; BAB13096.1; -; Genomic_DNA.
DR RefSeq; NP_240210.1; NC_002528.1.
DR RefSeq; WP_010896096.1; NC_002528.1.
DR AlphaFoldDB; P57473; -.
DR SMR; P57473; -.
DR STRING; 107806.10039062; -.
DR PRIDE; P57473; -.
DR EnsemblBacteria; BAB13096; BAB13096; BAB13096.
DR KEGG; buc:BU393; -.
DR PATRIC; fig|107806.10.peg.407; -.
DR eggNOG; COG0541; Bacteria.
DR HOGENOM; CLU_009301_6_0_6; -.
DR OMA; DTAGRHK; -.
DR Proteomes; UP000001806; 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: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 Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11564; PTHR11564; 1.
DR PANTHER; PTHR11564:SF7; PTHR11564:SF7; 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; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00959; ffh; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..451
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101150"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT CONFLICT 17
FT /note="L -> I (in Ref. 1; CAB90997)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="H -> N (in Ref. 1; CAB90997)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="I -> T (in Ref. 1; CAB90997)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="I -> L (in Ref. 1; CAB90997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 51200 MW; 6C6DF55FD9268A2C CRC64;
MFNNLTQRLS DSLKKILNKG RLTEENIKET IREVRKALLE ADVALSVIKK FIENVKKKSI
GHEINKSLTP GQEFIKIVKH ELIFAMGEKN HSLNFSIEPP AVILVVGLQG SGKTTSLAKL
GKWIKNKYKK KILITSTDTY RAAAIEQLKI LSDQIEIDFF ESDKHHTPIE ITKNAIKYAK
LKLYDVLLID TAGRLHIDKK MMNEIQQIQV ISKAIETLLI VDSMMGQDAI NMAKIFNNDL
LISGIILTKT DGDSRSGIAL SMRYITGKPI KFIGTGEKII SLEPFHPERI ADRILGMNDI
MSLIEDIEEK VDQSQIQKLT KKLKKGHDFN LNDFLTQIKQ MKKIGGLNYF ANKFSINHQL
SNNISLLNTD KNTLKKIEAM ICSMTPKERI KPIIIKGSRK RRIALGSGTQ IQDVNKLLKN
FDDIRRIMKK IKTDGIAKVI RGIKNMLPKK F
