ID   SECY2_LACKZ             Reviewed;         410 AA.
AC   F6CFW7;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Protein translocase subunit SecY 2 {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=WANG_p1049;
OS   Lactobacillus kefiranofaciens (strain ZW3).
OG   Plasmid pWW1.
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}.
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DR   EMBL; CP002765; AEG41652.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6CFW7; -.
DR   SMR; F6CFW7; -.
DR   PRIDE; F6CFW7; -.
DR   KEGG; lke:WANG_p1049; -.
DR   HOGENOM; CLU_030313_0_1_9; -.
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; 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..410
FT                   /note="Protein translocase subunit SecY 2"
FT                   /id="PRO_0000414206"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   410 AA;  45057 MW;  491A798446CCE3B7 CRC64;
     MILIIYRALF FVTIPGVNSA ALAKLSNNSS LTMLSMFSGG GFENFSIMSL GVTAYITAQI
     IVQLLQADVI PTFTQWSKEG QTGRKKLDQV TRSLTLVLGL VQATGITLGI NTLTNGKFMI
     ENNPFTIIVI AVSMTAGSFI AMWLGDLITE NGLGNGISVI ITAGILVRFP SMINDVIKGV
     TFGTKVNWIR FSELMIGAAI LILLIVWFTR SELRIPIQYA RRAQLTGKDS YLPLKIIVPG
     VIPVIFASTI MTIPQTILMF FNAGQNSSWY RVVQTFFTLS TTSGVIIYGL MIIFFEYLYS
     IVQIEPDKFA DNLEKQEAYI PNVYPGDPTK EFIQNMLNYL SLPGSLFLML VSIIPLLVAN
     SVSSSLQIGL SGSSILIITG VLIEIGRQIK GLKLKREYGT FLSTDFSLDD