FTSY_STRMU
ID FTSY_STRMU Reviewed; 498 AA.
AC Q8CWX8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; OrderedLocusNames=SMU_744;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=NG8;
RX PubMed=16293689; DOI=10.1073/pnas.0508778102;
RA Hasona A., Crowley P.J., Levesque C.M., Mair R.W., Cvitkovitch D.G.,
RA Bleiweis A.S., Brady L.J.;
RT "Streptococcal viability and diminished stress tolerance in mutants lacking
RT the signal recognition particle pathway or YidC2.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17466-17471(2005).
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 -!- 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 -!- DISRUPTION PHENOTYPE: Doubling time increases for growth under
CC nonstress conditions, unable to initiate growth at pH 5.0 and under
CC 3.5% NaCl salt stress. Double deletions of FtsY and Ffh, or FtsY and
CC YidC2 are barely able to grow in the absence of stress.
CC {ECO:0000269|PubMed:16293689}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR EMBL; AE014133; AAN58468.1; -; Genomic_DNA.
DR RefSeq; NP_721162.1; NC_004350.2.
DR RefSeq; WP_002263634.1; NC_004350.2.
DR AlphaFoldDB; Q8CWX8; -.
DR SMR; Q8CWX8; -.
DR STRING; 210007.SMU_744; -.
DR PRIDE; Q8CWX8; -.
DR EnsemblBacteria; AAN58468; AAN58468; SMU_744.
DR KEGG; smu:SMU_744; -.
DR PATRIC; fig|210007.7.peg.658; -.
DR eggNOG; COG0552; Bacteria.
DR HOGENOM; CLU_009301_2_1_9; -.
DR OMA; GMMEEQF; -.
DR PhylomeDB; Q8CWX8; -.
DR Proteomes; UP000002512; Chromosome.
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 3: Inferred from homology;
KW Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome.
FT CHAIN 1..498
FT /note="Signal recognition particle receptor FtsY"
FT /id="PRO_0000415445"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301..308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 383..387
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT BINDING 447..450
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
SQ SEQUENCE 498 AA; 55184 MW; 1033D2C13477D424 CRC64;
MGLFNRLFGK KRQEEKSTTD SIEEAAEQEV TQEKPALLAE TAETAESQQS VYEKDVTESQ
AEQVSDARII EDGQNSKEPA ASGHSVQEHK QQPVQHQQEV FHSENSVAAV QNNTETMPSQ
QKKDEKPNQS PDFMAEYYAR KAELAQKVES QKPAETAEQE SQTTLSDQKE TETAVNQSEE
EASSQIAESV ESEEEKYNRS LKKTRTGFGA RLNAFLANFR NVDEEFFEDL EEMLILSDVG
VQVASTLTED LRYEAKLEKA KKPEALRRVI IEKLVDIYDK DGQFNEKINF QNDLTVMLFV
GVNGVGKTTS IGKLAYKYKH QGKKVMLVAA DTFRAGAVAQ LAEWGRRVDV PVVTGPKNAD
PASVVYDGVE RAVAADVDIL MIDTAGRLQN KDNLMAELEK IGRVVKRVIP DAPHETLLTL
DASTGQNALV QAKEFSKITP LTGLILTKID GTAKGGVVLA IRQELAIPVK FIGFGEKIDD
IGEFHSEDFM RGLLEGLL
