ID   FTSY_MYCPN              Reviewed;         348 AA.
AC   P75362;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-JUN-2026, entry version 135.
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};
GN   OrderedLocusNames=MPN_425; ORFNames=MP416;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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 + phosphate + H(+); 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 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; U00089; AAB96064.1; -; Genomic_DNA.
DR   PIR; S73742; S73742.
DR   RefSeq; WP_010874781.1; NC_000912.1.
DR   AlphaFoldDB; P75362; -.
DR   SMR; P75362; -.
DR   STRING; 272634.MPN_425; -.
DR   PaxDb; 272634-MPN_425; -.
DR   EnsemblBacteria; AAB96064; AAB96064; MPN_425.
DR   GeneID; 66608908; -.
DR   KEGG; mpn:MPN_425; -.
DR   PATRIC; fig|272634.6.peg.460; -.
DR   HOGENOM; CLU_009301_3_0_14; -.
DR   OrthoDB; 9804720at2; -.
DR   BioCyc; MPNE272634:G1GJ3-688-MONOMER; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005047; F:signal recognition particle binding; IEA:TreeGrafter.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   FunFam; 3.40.50.300:FF:000053; Signal recognition particle receptor 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   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   NCBIfam; TIGR00064; ftsY; 1.
DR   PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43134:SF1; 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   SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome.
FT   CHAIN           1..348
FT                   /note="Signal recognition particle receptor FtsY"
FT                   /id="PRO_0000101137"
FT   BINDING         143..150
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         225..229
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         289..292
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ   SEQUENCE   348 AA;  38776 MW;  8A14C4DB9E1EAE29 CRC64;
     MSFIHKLIQK FKPKKKLVDQ VQQAVQEKSF FQANQKSYYQ GLNKSANSFA NTINKLAANY
     VTVNEQFQES LFEELVLLDI GYHAATKICD AIVQELKLQR VSDPQLIQEI IVDKLIVYYI
     QDKLFETDLT VEANKTNVYL FVGVNGVGKT TSLAKLADQL TKQNKRVLMV AGDTFRAGAV
     AQLAEWAQRI GCDIVLPNPK EETPAVIFRG VQQGIQNEYD FVLCDTSGRL QNKTNLMNEL
     KKIYQIVQKV SSAKPQETLL VLDGTTGQSG LAQAKVFNEF TELTGIILTK MDSSSKGGII
     LAIKDLFNLP VKLIGFGETT ADLAAFDLEQ YVLGLTKNLS LNHEPNQT
//