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 03-AUG-2022, entry version 144.
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).
RN [6]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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 (By similarity).
CC Interacts with FloT (PubMed:23651456). {ECO:0000255|HAMAP-
CC Rule:MF_01465, ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456};
CC Multi-pass membrane protein. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:23651456}.
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};
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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 AlphaFoldDB; P16336; -.
DR SMR; P16336; -.
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; BSU_01360.
DR GeneID; 936779; -.
DR KEGG; bsu:BSU01360; -.
DR PATRIC; fig|224308.179.peg.139; -.
DR eggNOG; COG0201; Bacteria.
DR InParanoid; P16336; -.
DR OMA; FAMWLGE; -.
DR PhylomeDB; P16336; -.
DR BioCyc; BSUB:BSU01360-MON; -.
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:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
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
