ID   SECY1_LACKZ             Reviewed;         431 AA.
AC   F6CD01;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Protein translocase subunit SecY 1 {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=WANG_0015;
OS   Lactobacillus kefiranofaciens (strain ZW3).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1033837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZW3;
RX   PubMed=21705607; DOI=10.1128/jb.05306-11;
RA   Wang Y., Wang J., Ahmed Z., Bai X., Wang J.;
RT   "Complete genome sequence of Lactobacillus kefiranofaciens ZW3.";
RL   J. Bacteriol. 193:4280-4281(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002764; AEG39710.1; -; Genomic_DNA.
DR   RefSeq; WP_013853513.1; NC_015602.1.
DR   AlphaFoldDB; F6CD01; -.
DR   SMR; F6CD01; -.
DR   KEGG; lke:WANG_0015; -.
DR   HOGENOM; CLU_030313_0_1_9; -.
DR   OMA; FAMWLGE; -.
DR   OrthoDB; 1567535at2; -.
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; Plasmid; Protein transport; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..431
FT                   /note="Protein translocase subunit SecY 1"
FT                   /id="PRO_0000414205"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   431 AA;  47691 MW;  6C2953CE6D4F3AD1 CRC64;
     MFSTLKNAFK DKEIRNKIYF TLFILLLYRI GANITVPGIN VKAITQVAQT GLVPMLDTVS
     GGGLDNYSIF SLGVSPYITA QIVIQLLQMD IVPTLVEWGK QGEVGRRKTN QVTRYLTLVV
     AFVQSIGITL GFNALTQMGL VKNQTPQTYV EIAIIMTAGT MLLTWLGDEI TDKGLGNGVS
     VIIFAGIIAR LPSGLYQIYK EEIINNSASD RWQGILFFIA VIVAILIVTQ LVTWVEQADR
     RIPIQYTRRA TISGSESFLP LKVNVSGVIP VIFASSFIVT PATILMAFQR TQGDQQWFKV
     MNQIFSLQTT PGVIIYTLLI ILFTFFYAFV QVNPEKLAEN LQKQGAYIPS VWPGKDTQDY
     VSKMLIKLST VGSIFLGLVA LLPQLATNFW NLPSSIGLGG TSLLIVIGVV LELSRQINGL
     LMKREYVGFI R