(data stored in SCRATCH3701 zone)

SWISSPROT: SRP54_RICTY

ID   SRP54_RICTY             Reviewed;         449 AA.
AC   Q68XJ4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 98.
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=RT0164;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03648.1; -; Genomic_DNA.
DR   RefSeq; WP_011190635.1; NC_006142.1.
DR   SMR; Q68XJ4; -.
DR   STRING; 257363.RT0164; -.
DR   PRIDE; Q68XJ4; -.
DR   EnsemblBacteria; AAU03648; AAU03648; RT0164.
DR   KEGG; rty:RT0164; -.
DR   eggNOG; ENOG4105CB9; Bacteria.
DR   eggNOG; COG0541; LUCA.
DR   HOGENOM; HOG000036164; -.
DR   KO; K03106; -.
DR   OMA; DTAGRHK; -.
DR   OrthoDB; 656414at2; -.
DR   BioCyc; RTYP257363:G1G0L-168-MONOMER; -.
DR   Proteomes; UP000000604; 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   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;
DR   PRODOM; Q68XJ4.
DR   SWISS-2DPAGE; Q68XJ4.
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   CHAIN           1..449
FT                   /note="Signal recognition particle protein"
FT                   /id="PRO_0000286500"
FT   NP_BIND         109..116
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   NP_BIND         191..195
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
FT   NP_BIND         249..252
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00306"
SQ   SEQUENCE   449 AA;  49352 MW;  038C38E51ADAE908 CRC64;
     MFKTLTQNLT KIFDRLVNSG ILTENQIDTA MRDVRVALLE SDVALPVIKG FIAEVKQKAL
     GQEVIKSVSP GQMIIKIIHE EMINLLASSE STTKLNLNSK PPVNLLMVGL QGGGKTTASG
     KLALLLKNQN KKVLLVSLDT YRPAAQEQLA IIANSVNIDS LPIVQGEQPL DIVKRAISEA
     KIFAYDVVIY DTAGRIQIDN VMMEEALAIK KILNPTETLL VIDSMTGQDA VVTARSFSDK
     LEISGLILSR IDGDTKGGAA LSVKYLTQKP IKFLSCGEKL TDLEEFDAER LASRILDMGD
     IISFVKKAAS IVDREEAERT AIKLKSGKFD LNDYLKHMRS IKKMGGFGSI LSMLPGSGKI
     IDQIDQSKLD SRIIEHQEAI ILSMTLKERK NPDIINASRR KRIAAGAGMT VQKVNILLKQ
     YKQISAVMKK ASKMNPQNLF RSGISKLFS
//

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