ID   SECY_LACLC              Reviewed;         439 AA.
AC   P27148;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 3.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MG1614;
RX   PubMed=1908794; DOI=10.1016/0014-5793(91)81015-z;
RA   Koivula T., Palva I., Hemilae H.;
RT   "Nucleotide sequence of the secY gene from Lactococcus lactis and
RT   identification of conserved regions by comparison of four SecY proteins.";
RL   FEBS Lett. 288:114-118(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 422-439.
RC   STRAIN=MG1614;
RX   PubMed=1783905; DOI=10.1099/00221287-137-11-2595;
RA   Koivula T., Hemilae H.;
RT   "Nucleotide sequence of a Lactococcus lactis gene cluster encoding
RT   adenylate kinase, initiation factor 1 and ribosomal proteins.";
RL   J. Gen. Microbiol. 137:2595-2600(1991).
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; X59250; CAA41939.1; -; Genomic_DNA.
DR   PIR; S17985; S17985.
DR   RefSeq; WP_011836021.1; NZ_LITG01000138.1.
DR   AlphaFoldDB; P27148; -.
DR   SMR; P27148; -.
DR   OMA; FAMWLGE; -.
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..439
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131728"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        269..289
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        373..393
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   439 AA;  48438 MW;  082A7639A05F04F3 CRC64;
     MFFKTLKEAF KVKDVRARIL FTIFILFVFR LGAHITAPGV NVQNLQQVAD LPFLSMMNLV
     SGNAMQNYSL FAMGVSPYIT ASIIVQLLQM DILPKFVEWS KQGEIGRRKL NQATRYITLV
     LAMAQSIGIT AGFQAMSSLN IVQNPNWQSY LMIGVLLTTG SMVVTWMGEQ INEKGFGSGV
     SVIIFAGIVS GIPSAIKSVY DEKFLNVRPS EIPMSWIFVI GLILSAIVII YVTTFVQQAE
     RKVPIQYTKL TQGAPTSSYL PLRVNPAGVI PVIFAGSITT APATILQFLQ RSQGSNVGWL
     STLQNALSYT TWTGMLFYAL LIVLFTFFYS FVQVNPEKMA ENLQKQGSYI PSVRPGKGTE
     KYVSRLLMRL ATVGSLFLGL ISIIPIAAQN VWGLPKIVAL GGTSLLILIQ VAIQAVKQLE
     GYLLKRKYAG FMDNPLETK