FTSY_NEIGO
ID FTSY_NEIGO Reviewed; 416 AA.
AC P14929;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920};
DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920};
GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; Synonyms=pilA;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11A;
RX PubMed=2854063; DOI=10.1002/j.1460-2075.1988.tb03335.x;
RA Taha M.K., So M., Seifert H.S., Billyard E., Marchal C.;
RT "Pilin expression in Neisseria gonorrhoeae is under both positive and
RT negative transcriptional control.";
RL EMBO J. 7:4367-4378(1988).
RN [2]
RP GTPASE ACTIVITY.
RX PubMed=7592800; DOI=10.1074/jbc.270.44.26045;
RA Arvidson C.G., So M.;
RT "The Neisseria transcriptional regulator PilA has a GTPase activity.";
RL J. Biol. Chem. 270:26045-26048(1995).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-307.
RX PubMed=9922234; DOI=10.1128/jb.181.3.731-739.1999;
RA Arvidson C.G., Powers T., Walter P., So M.;
RT "Neisseria gonorrhoeae PilA is an FtsY homolog.";
RL J. Bacteriol. 181:731-739(1999).
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, ECO:0000269|PubMed:9922234}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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 -!- MISCELLANEOUS: In vitro purified FtsY has been shown to bind to pilE
CC promoter DNA in a sequence-specific manner using gel retardation assay
CC but it cannot be explained.
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:2854063}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA32144.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X13965; CAA32144.1; ALT_FRAME; Genomic_DNA.
DR PIR; S02017; S02017.
DR AlphaFoldDB; P14929; -.
DR SMR; P14929; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
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; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43134:SF7; PTHR43134:SF7; 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.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Receptor.
FT CHAIN 1..416
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000101141"
FT REGION 1..24
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 224..231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 304..308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 368..371
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT MUTAGEN 307
FT /note="G->A: Decrease in GTPase activity; unable to
FT complement the lack of FtsY in E.coli; no translocation
FT activity."
FT /evidence="ECO:0000269|PubMed:9922234"
SQ SEQUENCE 416 AA; 44360 MW; ABD977BAFF79E4ED CRC64;
MFSFFRRKKK QETPALEEAQ VQETAAKVES EVAQIVGNIK EDVESLAESV KGRAESAVET
VSGAVEQVKE TVAEMPSEAG EAAERVESAK EAVAETVGEA VGQVQEAVAT TEEHKLGWAA
RLKQGLAKSR DKMAKSLAGV FGGGQIGEDL YEELETVLIT GDMGMEATEY LMKDVRGRVS
LKGLKDGNEL RGALKEALYD LIKPLEKPLV LPETKEPFVI MLAGINGAGK TTSIGKLAKY
FQAQGKSVLL AAGDTFRAAA REQLQAWGGR NNVTVISQTT GDSAAVCFDA VQAAKARIDI
VLADTAGRLP TQLHLMEEIK KVKRVLQKAI PGAPHEIIVV LDANIGQNAV NQVKAFDDAL
GLTGLIVTKL DGTAKGGILA ALASDRPVPV RYIGVGEGID DLRPFDARAF VDRLLD
