ID   SECY2_STRPA             Reviewed;         418 AA.
AC   A1C3L4;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Accessory Sec system protein translocase subunit SecY2;
GN   Name=secY2;
OS   Streptococcus parasanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=FW213;
RX   PubMed=16997950; DOI=10.1128/jb.00836-06;
RA   Wu H., Bu S., Newell P., Chen Q., Fives-Taylor P.;
RT   "Two gene determinants are differentially involved in the biogenesis of
RT   Fap1 precursors in Streptococcus parasanguis.";
RL   J. Bacteriol. 189:1390-1398(2007).
CC   -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC       required for correct glycosylation and export of Fap1, a serine-rich
CC       fimbrial adhesin. Potentially the central subunit of a protein
CC       translocation channel. {ECO:0000269|PubMed:16997950}.
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 (Potential). Part of the accessory SecA2/SecY2 protein
CC       translocation apparatus required to export cell wall proteins.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No effect on general protein secretion. Decreases
CC       the extent of glycosylation of serine-rich fimbrial adhesin Fap1, but
CC       the protein is still found on the cell surface. The partially
CC       glycosylated Fap1 is larger than the wild-type protein.
CC       {ECO:0000269|PubMed:16997950}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DQ990875; ABL73999.1; -; Genomic_DNA.
DR   RefSeq; WP_041826480.1; NZ_JYPA01000019.1.
DR   AlphaFoldDB; A1C3L4; -.
DR   SMR; A1C3L4; -.
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   Gene3D; 1.10.3370.10; -; 1.
DR   HAMAP; MF_01466; SecY2; 1.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR014269; SecY2.
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; TIGR02920; acc_sec_Y2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..418
FT                   /note="Accessory Sec system protein translocase subunit
FT                   SecY2"
FT                   /id="PRO_0000414877"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   418 AA;  47510 MW;  E94F50D632A4FAAA CRC64;
     MLRKLQKYWK KSIIFQRFTW MIGIVFIYML GRQIPIPTVG VDKVVVGNAS DSQLLENFGA
     ITGIQFSNMT LFSLGIGPTM TMMILWRFLI TFKLIGSWTS NKVNRLQFLL TLAIALLQSF
     GITNDSKFLL IFGYSHSTLR IITIILLTTG TFILNWLCKI NSERGIGGMT VVILVNMILT
     FQSNIIRYFS VQQFKFSSLI QYGLVFFVAL SILIWFNILL YKGEYRIPIQ RVGLNTPYHA
     SSYLPIRVTP AGAMPFMYGM TLMMLPPYIF VVLLHIFPGN QILEYLSVHI GLSQLPGVIC
     YIFLLYFLSI GFAYYNYDPY EISKNMRNNG DYISGKKPGE ETIKYIQYVV NSFAQFGAFT
     VIIFGGLPML AVLLQGQGKN SVSIALLISN AYIIVSLLLG VIEQVDTMNS WKKYKNLI