ID   SECY_MICLU              Reviewed;         436 AA.
AC   P33108;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2533272; DOI=10.1007/bf02602908;
RA   Ohama T., Muto A., Osawa S.;
RT   "Spectinomycin operon of Micrococcus luteus: evolutionary implications of
RT   organization and novel codon usage.";
RL   J. Mol. Evol. 29:381-395(1989).
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; X17524; CAA35567.1; -; Genomic_DNA.
DR   PIR; S29891; S29891.
DR   AlphaFoldDB; P33108; -.
DR   SMR; P33108; -.
DR   STRING; 1232675.GCA_000309825_02138; -.
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; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..436
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131729"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   436 AA;  47324 MW;  EA97A4687D524748 CRC64;
     MLKAIARIVR TPDLLRKIAF TLGLIAVYRM GDFVPATGVD YPAVQQCLAA GNAQGGLYSF
     VNMFSGGALL QVSVFALGIM PYITASIIVQ LLRVVIPRFE QLHQERRRGQ ATLTQYTRYL
     TLALALLQAT TMASLARTGA LLGCSLPLLR DGSILTVLLV VIALTTGCLI VMWFGERITE
     NGVGNGMSLL IFTSIAAGFP AGLGQVVQTQ GWRVFAIVMG IGLLTMLAIV FVEESQRRIP
     VQYAKRQIGS RTVGGSSTYI PVKVNMANVI PVIFASSVLM LPGILIQFNT PQDGSAPAPW
     ITWLSRYFGS GDHPVYMALY FLLIIGFTYF YVSITFNPVE ISDNMKRYGG FIPASAPAGP
     TERYLQYVIS RITFVVGALY LGIVAMIPLI AFAVIGTSQN FPLGGTSILI MVGVGLQTVK
     QVSAQMEQRH YEGLLR