ID   SECY2_STRGN             Reviewed;         407 AA.
AC   Q9AEU0;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Accessory Sec system protein translocase subunit SecY2 {ECO:0000255|HAMAP-Rule:MF_01466};
GN   Name=secY2 {ECO:0000255|HAMAP-Rule:MF_01466};
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA   Bensing B.A., Sullam P.M.;
RT   "An accessory sec locus of Streptococcus gordonii is required for export of
RT   the surface protein GspB and for normal levels of binding to human
RT   platelets.";
RL   Mol. Microbiol. 44:1081-1094(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M99;
RX   PubMed=15901716; DOI=10.1128/jb.187.11.3878-3883.2005;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Two additional components of the accessory sec system mediating export of
RT   the Streptococcus gordonii platelet-binding protein GspB.";
RL   J. Bacteriol. 187:3878-3883(2005).
CC   -!- FUNCTION: The central subunit of a protein translocation channel
CC       (Potential). Part of the accessory SecA2/SecY2 system specifically
CC       required to export GspB, a serine-rich repeat cell wall protein encoded
CC       upstream in the same operon. {ECO:0000269|PubMed:12010500,
CC       ECO:0000305}.
CC   -!- SUBUNIT: May form heterotrimers with SecE and SecG subunits
CC       (Potential). Component of the accessory SecA2/SecY2 protein translocase
CC       complex required to export cell wall protein GspB. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01466};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01466}.
CC   -!- DISRUPTION PHENOTYPE: Loss of adherence to human platelet cells, loss
CC       of export of cell wall protein GspB; GspB accumulates in the cytoplasm.
CC       {ECO:0000269|PubMed:12010500}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01466}.
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DR   EMBL; AY028381; AAK16997.1; -; Genomic_DNA.
DR   RefSeq; WP_061595683.1; NZ_LAWP01000001.1.
DR   AlphaFoldDB; Q9AEU0; -.
DR   SMR; Q9AEU0; -.
DR   TCDB; 3.A.5.10.1; the general secretory pathway (sec) family.
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..407
FT                   /note="Accessory Sec system protein translocase subunit
FT                   SecY2"
FT                   /id="PRO_0000414208"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
SQ   SEQUENCE   407 AA;  46158 MW;  9B516E14ADEE7E16 CRC64;
     MKSFFKPLIL KKFLWTLLFV FIYVLGSKLT LPFVDVSSIA KLNGDSVTLN YAAALMGGNL
     RSMSFFSIGL APWMSSILIW QMFTVSKRLG LNKLSMESQE KRRMLLTLAI ALIQSLGLVL
     NLPLKTVAGV GQGTIVFLDT LILIAGTYFL IWLTDLNSSM GLGGSIMIVM VSMISYIPQD
     IWLSIQELKI SPLILALIGF FSLCFLYLAV LVERAKYRIP INKINIHNRF KKYSYLDIRV
     NAAGGLPIMY AMTLVSIPQY FLMLLLFFQP NNRLLKEGIL SLAMGGIPWF ILYLLTIFIL
     AWAFAFINVN SDQIAERMQR SGEYIENLYP GEATRRYIHK TVGYFAFVGA LYLVLVAGLP
     MLLIFLDIRY MRLGMIPGMF MIFIGMVFSI KDEVDTLTLN DRYHSLF