ID   SECY_STRLI              Reviewed;         437 AA.
AC   P49977;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=66 / 1326;
RX   PubMed=8918265; DOI=10.1016/0378-1119(96)00229-6;
RA   Ostiguy S., Gilbert M., Shareck F., Kluepfel D., Morosoli R.;
RT   "Cloning and sequencing of the secY homolog from Streptomyces lividans
RT   1326.";
RL   Gene 176:265-267(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TK24;
RA   Kim S.O., Suh J.W.;
RT   "Molecular cloning and characterization of the secY homolog from
RT   Streptomyces lividans TK24.";
RL   Sanop Misaengmul Hakhoe Chi 26:110-116(1998).
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; U27324; AAC44590.1; -; Genomic_DNA.
DR   EMBL; AF071012; AAC33323.1; -; Genomic_DNA.
DR   PIR; JC5115; JC5115.
DR   AlphaFoldDB; P49977; -.
DR   SMR; P49977; -.
DR   PRIDE; P49977; -.
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..437
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131753"
FT   TRANSMEM        19..39
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        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        400..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   437 AA;  47312 MW;  95AB676AA9E46EF6 CRC64;
     MLTAFAPAFK TPDLRKKLLF TLGIIVVYRL GTHIPIPGVD YKNVQECVDQ ASGNQGLFGL
     VNMFSGGALL QITVFALGIM PYITASIILQ LLTVVIPRLE ALKKEGQAGT AKITQYTRYL
     TVALAILQGT GLVATARSGA LFSGCTVAGQ IVPDQAIFTT VVMVICMTAG TCVVMWLGEL
     ITDRGIGNGM SILMFISIAA TFPSALWAIK KQGELADGWI EFGTVILVGL VMVGLVVFVE
     QAQRRIPVQY AKRMIGRRSY GGTSTYIPLK VNQAGVIPVI FASSLLYIPA LIVQFSNSTA
     GWATWITKNL ADTAATPHII LYFFLIVFFA FFYVAISFNP EEVADNMKKY GGFIPGIRAG
     RPTAEYLSYV LNRITWPGSL YLGLIALVPT MALAGFGANQ NFPFGGTSIL IIVGVGLETV
     KQIESQLQQR NYEGFLR