ID   SECY_GEOSE              Reviewed;          99 AA.
AC   P28620;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein translocase subunit SecY;
DE   Flags: Fragment;
GN   Name=secY;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1554691; DOI=10.1021/bi00127a002;
RA   Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H.,
RA   Barzu O., Gilles A.M.;
RT   "Zinc, a novel structural element found in the family of bacterial
RT   adenylate kinases.";
RL   Biochemistry 31:3038-3043(1992).
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 (By
CC       similarity). {ECO:0000250}.
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR   EMBL; M88104; AAA22204.1; -; Genomic_DNA.
DR   PIR; A42196; A42196.
DR   AlphaFoldDB; P28620; -.
DR   SMR; P28620; -.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3370.10; -; 1.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR023201; SecY_dom_sf.
DR   PANTHER; PTHR10906; PTHR10906; 1.
DR   Pfam; PF00344; SecY; 1.
DR   SUPFAM; SSF103491; SSF103491; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           <1..99
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131710"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   99 AA;  10910 MW;  F33BB10867C7C88B CRC64;
     NPEQMAENLK KQGGYIPGIR PGKNTQEYVT RILYRLTLVG SVFLAVIAVL PVFFVNVANL
     PPSAKIGGTS LLIVVGVALE TMKQLESQLV KRHYRGFIK