(data stored in ACNUC7421 zone)

SWISSPROT: A8FPQ9_SHESH

ID   A8FPQ9_SHESH            Unreviewed;       540 AA.
AC   A8FPQ9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920};
DE            Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920};
GN   Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920};
GN   OrderedLocusNames=Ssed_0219 {ECO:0000313|EMBL:ABV34832.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34832.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34832.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34832.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in targeting and insertion of nascent membrane
CC       proteins into the cytoplasmic membrane. Acts as a receptor for the
CC       complex formed by the signal recognition particle (SRP) and the
CC       ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to
CC       the transfer of the RNC complex to the Sec translocase for
CC       insertion into the membrane, the hydrolysis of GTP by both Ffh and
CC       FtsY, and the dissociation of the SRP-FtsY complex into the
CC       individual components. {ECO:0000256|HAMAP-Rule:MF_00920}.
CC   -!- SUBUNIT: Part of the signal recognition particle protein
CC       translocation system, which is composed of SRP and FtsY. SRP is a
CC       ribonucleoprotein composed of Ffh and a 4.5S RNA molecule.
CC       {ECO:0000256|HAMAP-Rule:MF_00920}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00920}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00920}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_00920}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00920}.
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DR   EMBL; CP000821; ABV34832.1; -; Genomic_DNA.
DR   RefSeq; WP_012004358.1; NC_009831.1.
DR   ProteinModelPortal; A8FPQ9; -.
DR   STRING; 425104.Ssed_0219; -.
DR   EnsemblBacteria; ABV34832; ABV34832; Ssed_0219.
DR   KEGG; sse:Ssed_0219; -.
DR   eggNOG; ENOG4105CCP; Bacteria.
DR   eggNOG; COG0552; LUCA.
DR   HOGENOM; HOG000036278; -.
DR   KO; K03110; -.
DR   OMA; FTWSAMV; -.
DR   OrthoDB; POG091H021F; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   HAMAP; MF_00920; FtsY; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR004390; SR_rcpt_FtsY.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   PANTHER; PTHR43134:SF1; PTHR43134:SF1; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00962; SRP54; 1.
DR   SMART; SM00963; SRP54_N; 1.
DR   SUPFAM; SSF47364; SSF47364; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00064; ftsY; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPQ9.
DR   SWISS-2DPAGE; A8FPQ9.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00920};
KW   Receptor {ECO:0000256|HAMAP-Rule:MF_00920}.
FT   DOMAIN      236    316       SRP54_N. {ECO:0000259|SMART:SM00963}.
FT   DOMAIN      330    521       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      331    532       SRP54. {ECO:0000259|SMART:SM00962}.
FT   NP_BIND     338    345       GTP. {ECO:0000256|HAMAP-Rule:MF_00920}.
FT   NP_BIND     420    424       GTP. {ECO:0000256|HAMAP-Rule:MF_00920}.
FT   NP_BIND     484    487       GTP. {ECO:0000256|HAMAP-Rule:MF_00920}.
FT   COILED       33    216       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   540 AA;  58482 MW;  D37621987688F89D CRC64;
     MAKKGFFSWF RKDKSKDEVS APEAEVVTES QDAVEAEALS EEQAKQAEQA RIEAEALALA
     EEQAEQARIE AEALALAEEQ AKQAELARIE AEALALAEEQ AKQAEQARIE AEAAALAEEQ
     AKQAEQARIE AEAAALAEEQ AKQAEQARIE AEAAALAEEQ AKQAELARIE AEAAALAEEQ
     AKQAEQARIE TEAAALAEEQ AKQAELDAEQ VAAEQETEKQ PEPQEKPTKE GFFARLKRGL
     KRTSENIGSG FVSLFSGKKI DDDLFEELEE QLLIADVGVE TTTRLIDSLT EQASRKQLKD
     GEALYEILRD EMQKTLEPVS IPLVPESADG PFVILMVGVN GVGKTTTIGK LAKQYQAQGK
     SVMLAAGDTF RAAAVEQLQV WGQRNDIPVV AQHTGADSAS VLFDALQAAR ARNIDILIAD
     TAGRLQNKAH LMDELKKVIR VMKKQDESAP HEVMLTLDAS TGQNAISQAE LFKKAVGVTG
     ITISKLDGTA KGGVIFAIAD KFGIPIRHIG VGEQIDDLRT FDAKDFVDAL FTQESDENKS
//

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