ID   SECY_BUCBP              Reviewed;         441 AA.
AC   Q89A85;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=bbp_447;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 {ECO:0000255|HAMAP-Rule:MF_01465};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01465}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC       Rule:MF_01465}.
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DR   EMBL; AE016826; AAO27153.1; -; Genomic_DNA.
DR   RefSeq; WP_011091554.1; NC_004545.1.
DR   AlphaFoldDB; Q89A85; -.
DR   SMR; Q89A85; -.
DR   STRING; 224915.bbp_447; -.
DR   EnsemblBacteria; AAO27153; AAO27153; bbp_447.
DR   GeneID; 56470982; -.
DR   KEGG; bab:bbp_447; -.
DR   eggNOG; COG0201; Bacteria.
DR   HOGENOM; CLU_030313_0_2_6; -.
DR   OMA; FAMWLGE; -.
DR   OrthoDB; 1567535at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
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;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..441
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131716"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   441 AA;  49960 MW;  0066495E2CE49DF6 CRC64;
     MIKKKLETKL KNFGNQFSEL KQRMYFVIFS LIVFRMGSYI PIPGIDTVAL ASLLEHHRGT
     IIEMFNMFSG GALSRASIFA LGIMPFISSS IIVQILTLIH PKFIEMKKDG EQGRHRINKY
     IRYITLILAA LQSFGMSISL PNIPGLKDVI IDPSISFYGI AIISLITGTI FLMWLGELIT
     EKGIGNGISI IIFSGIVSGL PSSFLNTVEK VRQGSLHVLL FCFIGIVIFL VTLLVVYIER
     SQRKITISYA KRNLGHRTYS MNSTHLPLKL NMSGVIPAIF ASSIVLFPAT IASWFGNRDH
     FKWLVDIVFY LQPTKPLYIL TYITAIIFFC FFYTGLAFNP RETADNLKKS GAFILGIRPG
     EKTAQYINKI MLRLTFLGSM YMAFICLVPE LMRFFMDVPF YFGGTSLLII VVVIIDFISQ
     VQTYIMSTQY ESVLKKNKFR F