(data stored in ACNUC7421 zone)

SWISSPROT: SECY_BACSU

ID   SECY_BACSU              Reviewed;         431 AA.
AC   P16336;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   11-DEC-2019, entry version 135.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=BSU01360;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=2110998; DOI=10.1111/j.1365-2958.1990.tb00597.x;
RA   Suh J.-W., Boylan S.A., Thomas S.M., Dolan K.M., Oliver D.B., Price C.W.;
RT   "Isolation of a secY homologue from Bacillus subtilis: evidence for a
RT   common protein export pathway in eubacteria.";
RL   Mol. Microbiol. 4:305-314(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2139212; DOI=10.1093/nar/18.6.1647;
RA   Yoshikawa H., Doi R.H.;
RT   "Sequence of the Bacillus subtilis spectinomycin resistance gene region.";
RL   Nucleic Acids Res. 18:1647-1647(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2113521; DOI=10.1093/oxfordjournals.jbchem.a123093;
RA   Nakamura K., Nakamura A., Takamatsu H., Yoshikawa H., Yamane K.;
RT   "Cloning and characterization of a Bacillus subtilis gene homologous to E.
RT   coli secY.";
RL   J. Biochem. 107:603-607(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA   Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT   "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT   alpha region.";
RL   Gene 169:17-23(1996).
RN   [5]
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).
CC   -!- FUNCTION: The central subunit of the protein translocation channel
CC       SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC       domains form a lateral gate at the front which open onto the bilayer
CC       between TMs 2 and 7, and are clamped together by SecE at the back. The
CC       channel is closed by both a pore ring composed of hydrophobic SecY
CC       resides and a short helix (helix 2A) on the extracellular side of the
CC       membrane which forms a plug. The plug probably moves laterally to allow
CC       the channel to open. The ring and the pore may move independently.
CC       {ECO:0000255|HAMAP-Rule:MF_01465}.
CC   -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC       consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC       oligomers, although 1 heterotrimer is thought to be able to translocate
CC       proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC       proteins may be involved. Interacts with SecA. {ECO:0000255|HAMAP-
CC       Rule:MF_01465}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC       Rule:MF_01465}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA00495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; X51329; CAA35712.1; -; Genomic_DNA.
DR   EMBL; M31102; AAB59118.1; -; Genomic_DNA.
DR   EMBL; D00619; BAA00495.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L47971; AAB06819.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11912.1; -; Genomic_DNA.
DR   PIR; S08629; BWBSSY.
DR   RefSeq; NP_388017.1; NC_000964.3.
DR   RefSeq; WP_004399662.1; NZ_JNCM01000029.1.
DR   STRING; 224308.BSU01360; -.
DR   TCDB; 3.A.5.2.1; the general secretory pathway (sec) family.
DR   PaxDb; P16336; -.
DR   PRIDE; P16336; -.
DR   EnsemblBacteria; CAB11912; CAB11912; BSU01360.
DR   GeneID; 936779; -.
DR   KEGG; bsu:BSU01360; -.
DR   PATRIC; fig|224308.179.peg.139; -.
DR   eggNOG; ENOG4105CGG; Bacteria.
DR   eggNOG; COG0201; LUCA.
DR   HOGENOM; HOG000080586; -.
DR   InParanoid; P16336; -.
DR   KO; K03076; -.
DR   OMA; FIMWLGE; -.
DR   PhylomeDB; P16336; -.
DR   BioCyc; BSUB:BSU01360-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR   Gene3D; 1.10.3370.10; -; 1.
DR   HAMAP; MF_01465; SecY; 1.
DR   InterPro; IPR026593; SecY.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR030659; SecY_CS.
DR   InterPro; IPR023201; SecY_dom_sf.
DR   PANTHER; PTHR10906; PTHR10906; 1.
DR   Pfam; PF00344; SecY; 1.
DR   PIRSF; PIRSF004557; SecY; 1.
DR   SUPFAM; SSF103491; SSF103491; 1.
DR   TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR   PROSITE; PS00755; SECY_1; 1.
DR   PROSITE; PS00756; SECY_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; P16336.
DR   SWISS-2DPAGE; P16336.
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..431
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131711"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        39..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        88..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        137..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        167..177
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        199..213
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        235..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        283..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        330..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TOPO_DOM        411..431
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  47243 MW;  6AB949378D17D8B4 CRC64;
     MFKTISNFMR VSDIRNKIIF TLLMLIVFRI GAFIPVPYVN AEALQAQSQM GVFDLLNTFG
     GGALYQFSIF AMGITPYITA SIIIQLLQMD VVPKFTEWSK QGEVGRRKLA QFTRYFTIVL
     GFIQALGMSY GFNNLANGML IEKSGVSTYL IIALVLTGGT AFLMWLGEQI TSHGVGNGIS
     IIIFAGIVSS IPKTIGQIYE TQFVGSNDQL FIHIVKVALL VIAILAVIVG VIFIQQAVRK
     IAIQYAKGTG RSPAGGGQST HLPLKVNPAG VIPVIFAVAF LITPRTIASF FGTNDVTKWI
     QNNFDNTHPV GMAIYVALII AFTYFYAFVQ VNPEQMADNL KKQGGYIPGV RPGKMTQDRI
     TSILYRLTFV GSIFLAVISI LPIFFIQFAG LPQSAQIGGT SLLIVVGVAL ETMKQLESQL
     VKRNYRGFMK N
//

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