ID FTSY_NEIMC Reviewed; 421 AA.
AC O30391;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 105.
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}; Synonyms=pilA;
OS Neisseria meningitidis serogroup C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=135720;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8013.6 / Serogroup C;
RX PubMed=9434748; DOI=10.1006/abbi.1997.0399;
RA Arvidson C.G., So M.;
RT "Isolation and biochemical characterization of the PilA protein of
RT Neisseria meningitidis.";
RL Arch. Biochem. Biophys. 348:357-362(1997).
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 the
CC transfer of the RNC complex to the Sec translocase for insertion into
CC the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the
CC dissociation of the SRP-FtsY complex into the individual components.
CC {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. SRP is a ribonucleoprotein
CC composed of Ffh and a 4.5S RNA molecule. {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}.
CC -!- CAUTION: Was originally thought to activate the pilin promoter.
CC {ECO:0000305|PubMed:9434748}.
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DR EMBL; AF003940; AAB97510.1; -; Genomic_DNA.
DR PIR; T44429; T44429.
DR AlphaFoldDB; O30391; -.
DR SMR; O30391; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd17874; FtsY; 1.
DR Gene3D; 1.20.120.20; Apolipoprotein; 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: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 SUPFAM; SSF58113; Apolipoprotein A-I; 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.
FT CHAIN 1..421
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101144"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228..235
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 309..313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 373..376
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ SEQUENCE 421 AA; 45228 MW; C7CE70046AEBD91A CRC64;
MFSFFRRKKK QETPAPEEAQ IQETVAKVES EVAQIVENIK EDAESLAESV KGQVESAVET
VSGAVEQVKE TVAEMLSEAE EAAEKAAEQV EAAKEAVAET VGEAVGQVQE AVATTEEHKL
GWAARLKQGL TKSRDKMAKS LAGVFGGGQI DEDLYEELET VLITSDMDME ATEYLMKDVR
DRVSLKGLKD GNELRGALKE ALYDLIKPLE KPLVLPETKE PFVIMLAGIN GAGKTTSIGK
LAKYFQAQGK SVLLAAGDTF RAAAREQLQA WGERNNVTVI SQTTGDSAAV CFDAVQAAKA
RGIDIVLADT AGRLPTQLHL MEEIKKVKRV LQKAMPDAPH EIIVVLDANI GQNAVNQVKA
FDDALGLTGL IVTKLDGTAK GGILAALASD RPVPVRYIGV GEGIDDLRPF DARAFVDALL
D
//
