ID FTSY_AQUAE Reviewed; 461 AA.
AC O67066;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
DE EC=3.6.5.4 {ECO:0000255|HAMAP-Rule:MF_00920};
GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; OrderedLocusNames=aq_920;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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). {ECO:0000255|HAMAP-Rule:MF_00920}.
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:0000255|HAMAP-Rule:MF_00920};
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_00920}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR EMBL; AE000657; AAC07030.1; -; Genomic_DNA.
DR PIR; G70379; G70379.
DR RefSeq; NP_213628.1; NC_000918.1.
DR RefSeq; WP_010880566.1; NC_000918.1.
DR AlphaFoldDB; O67066; -.
DR SMR; O67066; -.
DR STRING; 224324.aq_920; -.
DR EnsemblBacteria; AAC07030; AAC07030; aq_920.
DR KEGG; aae:aq_920; -.
DR PATRIC; fig|224324.8.peg.721; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0552; Bacteria.
DR HOGENOM; CLU_009301_3_5_0; -.
DR InParanoid; O67066; -.
DR OrthoDB; 9804720at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd17874; FtsY; 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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00064; ftsY; 1.
DR PANTHER; PTHR43134:SF7; CELL DIVISION PROTEIN FTSY HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 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 SMART; SM00028; TPR; 1.
DR SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00300; SRP54; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding; Hydrolase;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; TPR repeat.
FT CHAIN 1..461
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101126"
FT REPEAT 105..138
FT /note="TPR"
FT BINDING 267..274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 349..353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 413..416
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ SEQUENCE 461 AA; 51931 MW; 9D66F143849A662F CRC64;
MVFFWRKSDV EKKAEKGDKN AILELIKQGK KEKAEKILKK YASQREDLAE LLFELYVQEG
KLVQAYPLLK KYGDKIGKAK ERAKVYQAVG EYQKAIEEFL KVGDFESLYN VAKIYHQLEK
PDKALEYAQR AEKLVPYEKK EELENFITQL KKELGLIEEK KESILDKLRR GLQKTKEAVE
FGVLFRGRKV DEEFFEELEE MLVKADVGVK TAVELTEKLR KEAIRKNIKE GEKIKELLKK
ELKELLKNCQ GELKIPEKVG AVLLFVGVNG SGKTTTIGKL AHQLKQKGKK VLLVAGDTFR
AAAIEQLEVW AKRAGVDIVK KEEGSDPGAV VYEGMKKAKE EGYEVVLVDT AGRLHTKEPL
INELRKIKKV IQKFDKEEPS ETLLVIDATT GQNAIQQAKV FKEAVDITGI VVTKLDGSAK
GGAVVAICRE LKIPIKLVGV GEGIDDLQPF DADAYVEALL E
//
