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Database: UniProt
Entry: FTSY_BACSU
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ID   FTSY_BACSU              Reviewed;         329 AA.
AC   P51835; O31736;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   27-MAR-2024, entry version 151.
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=srb;
GN   OrderedLocusNames=BSU15950;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584053; DOI=10.1093/dnares/2.2.95;
RA   Oguro A., Kakeshita H., Honda K., Takamatsu H., Nakamura K., Yamane K.;
RT   "srb: a Bacillus subtilis gene encoding a homologue of the alpha-subunit of
RT   the mammalian signal recognition particle receptor.";
RL   DNA Res. 2:95-100(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=8654983; DOI=10.1016/0378-1119(96)00181-3;
RA   Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.;
RT   "The effect of Srb, a homologue of the mammalian SRP receptor alpha-
RT   subunit, on Bacillus subtilis growth and protein translocation.";
RL   Gene 172:17-24(1996).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / PY79;
RX   PubMed=15995216; DOI=10.1128/jb.187.14.5000-5002.2005;
RA   Rubio A., Jiang X., Pogliano K.;
RT   "Localization of translocation complex components in Bacillus subtilis:
RT   enrichment of the signal recognition particle receptor at early sporulation
RT   septa.";
RL   J. Bacteriol. 187:5000-5002(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   -!- 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 membrane {ECO:0000255|HAMAP-Rule:MF_00920,
CC       ECO:0000269|PubMed:15995216}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00920, ECO:0000269|PubMed:15995216};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00920,
CC       ECO:0000269|PubMed:15995216}. Cytoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_00920, ECO:0000269|PubMed:15995216}. Note=Transiently localizes
CC       to early sporulation septa during sporulation.
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00920}.
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DR   EMBL; D49781; BAA08616.1; -; Genomic_DNA.
DR   EMBL; D64116; BAA10978.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13468.1; -; Genomic_DNA.
DR   PIR; JC4093; JC4093.
DR   RefSeq; NP_389477.1; NC_000964.3.
DR   RefSeq; WP_003232026.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P51835; -.
DR   SMR; P51835; -.
DR   STRING; 224308.BSU15950; -.
DR   jPOST; P51835; -.
DR   PaxDb; 224308-BSU15950; -.
DR   EnsemblBacteria; CAB13468; CAB13468; BSU_15950.
DR   GeneID; 936921; -.
DR   KEGG; bsu:BSU15950; -.
DR   PATRIC; fig|224308.179.peg.1735; -.
DR   eggNOG; COG0552; Bacteria.
DR   InParanoid; P51835; -.
DR   OrthoDB; 9804720at2; -.
DR   PhylomeDB; P51835; -.
DR   BioCyc; BSUB:BSU15950-MONOMER; -.
DR   Proteomes; UP000001570; 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   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; 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   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Signal recognition particle receptor FtsY"
FT                   /id="PRO_0000101127"
FT   BINDING         127..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         209..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   BINDING         273..276
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00920"
FT   CONFLICT        238
FT                   /note="A -> T (in Ref. 1; BAA08616/BAA10978)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  36343 MW;  295F7D6618594B78 CRC64;
     MSFFKKLKEK ITKQTDSVSE KFKDGLEKTR NSFQNKVNDL VSRYRKVDED FFEELEEVLI
     SADVGFTTVM ELIDELKKEV KRRNIQDPKE VQSVISEKLV EIYNSGDEQI SELNIQDGRL
     NVILLVGVNG VGKTTTIGKL AHKMKQEGKS VVLAAGDTFR AGAIEQLEVW GERTGVPVIK
     QTAGSDPAAV IYDAVHAAKA RNADVLICDT AGRLQNKVNL MKELEKVKRV IEREVPEAPH
     EVLLALDATT GQNAMAQAKE FSKATNVTGI ALTKLDGTAK GGIVLAIRNE LHIPVKLVGL
     GEKVDDLQEF DPESYVYGLF SDLVEKADD
//
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