SRP54_SYNE7
ID SRP54_SYNE7 Reviewed; 485 AA.
AC Q55311; Q31MB8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
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};
GN OrderedLocusNames=Synpcc7942_1771;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8605315; DOI=10.1007/bf00049341;
RA Packer J.C.L., Howe C.J.;
RT "The cyanobacterial genome contains a single copy of the ffh gene encoding
RT a homologue of the 54 kDa subunit of signal recognition particle.";
RL Plant Mol. Biol. 30:659-665(1996).
RN [2]
RP ERRATUM OF PUBMED:8605315.
RX PubMed=8756611;
RA Packer J.C.L., Howe C.J.;
RL Plant Mol. Biol. 31:659-665(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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:0000255|HAMAP-Rule:MF_00306}.
CC -!- SUBUNIT: Part of the signal recognition particle protein translocation
CC system, which is composed of SRP and FtsY. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB57801.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X92071; CAA63054.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57801.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039755651.1; NC_007604.1.
DR AlphaFoldDB; Q55311; -.
DR SMR; Q55311; -.
DR STRING; 1140.Synpcc7942_1771; -.
DR PRIDE; Q55311; -.
DR EnsemblBacteria; ABB57801; ABB57801; Synpcc7942_1771.
DR KEGG; syf:Synpcc7942_1771; -.
DR eggNOG; COG0541; Bacteria.
DR HOGENOM; CLU_009301_6_0_3; -.
DR OrthoDB; 656414at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1771-MON; -.
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; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..485
FT /note="Signal recognition particle protein"
FT /id="PRO_0000101168"
FT REGION 452..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
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:0000255|HAMAP-Rule:MF_00306"
FT BINDING 189..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ SEQUENCE 485 AA; 52820 MW; 789F3509127537AA CRC64;
MFDALAERLE QAWTKLRGQD KISESNVQEA LKEVRRALLE ADVNLGVVKE FIAQVQEKAV
GTQVISGIRP DQQFIKVVYD ELVQVMGETH VPLAQAAKAP TVILMAGLQG AGKTTATAKL
ALHLRKEGRS TLLVATDVYR PAAIDQLITL GKQIDVPVFE LGSDANPVEI ARQGVEKARQ
EGIDTVIVDT AGRLQIDTEM MEELAQVKEA IAPHEVLLVV DSMIGQEAAS LTRSFHERIG
ITGAILTKLD GDSRGGAALS IRRVSGQPIK FVGLGEKVEA LQPFHPERMA SRILGMGDVL
TLVEKAQEEI DLADVEKMQE KILAAKFDFT DFLKQMRLLK NMGSLAGFIK LIPGLGGKIN
DEQLRQGERQ LKRVEAMINS MTPQERRDPD LLSNSPSRRH RIAKGCGQTE AEIRQIIQQF
QQMRTMMQQM SQGGFPGMGG MGMPGFGGGM PGFGGGAPAP QPGFRGYGPP KKQKKGSKKK
KGFGL
