SECY2_STAA8
ID SECY2_STAA8 Reviewed; 403 AA.
AC Q2FUW2;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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};
GN OrderedLocusNames=SAOUHSC_02989;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ISP479C;
RX PubMed=18621893; DOI=10.1128/jb.00300-08;
RA Siboo I.R., Chaffin D.O., Rubens C.E., Sullam P.M.;
RT "Characterization of the accessory Sec system of Staphylococcus aureus.";
RL J. Bacteriol. 190:6188-6196(2008).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=RN4220, and SH1000;
RX PubMed=20472795; DOI=10.1128/jb.01452-09;
RA Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA van Dijl J.M.;
RT "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT Staphylococcus aureus.";
RL J. Bacteriol. 192:3788-3800(2010).
CC -!- FUNCTION: The central subunit of a protein translocation channel
CC (Potential). Part of the accessory SecA2/SecY2 system specifically
CC required to export SraP, a serine-rich repeat cell wall protein encoded
CC upstream in the same operon. {ECO:0000269|PubMed:18621893,
CC ECO:0000269|PubMed:20472795, 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 SrpA. {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: No effect on cell growth, significantly reduces
CC export of the cell wall protein SraP. The small amount that is exported
CC seems to be glycosylated normally. A double secG/secY2 mutant enters
CC stationary phase earlier and has significant differences in the export
CC pattern of a number of extracellular proteins (shown in RN4220). Single
CC or double deletions are as virulent as wild-type (shown in RN4220 and
CC SH1000). {ECO:0000269|PubMed:18621893, ECO:0000269|PubMed:20472795}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01466}.
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DR EMBL; CP000253; ABD31976.1; -; Genomic_DNA.
DR RefSeq; WP_000916119.1; NZ_LS483365.1.
DR RefSeq; YP_501438.1; NC_007795.1.
DR AlphaFoldDB; Q2FUW2; -.
DR SMR; Q2FUW2; -.
DR STRING; 1280.SAXN108_2924; -.
DR EnsemblBacteria; ABD31976; ABD31976; SAOUHSC_02989.
DR GeneID; 3921471; -.
DR KEGG; sao:SAOUHSC_02989; -.
DR PATRIC; fig|93061.5.peg.2696; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_4_0_9; -.
DR OMA; YSYLEIM; -.
DR PRO; PR:Q2FUW2; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..403
FT /note="Accessory Sec system protein translocase subunit
FT SecY2"
FT /id="PRO_0000414207"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
SQ SEQUENCE 403 AA; 46885 MW; 0E2EF27001CC8327 CRC64;
MLKLLQQYEY KIIYKRMLYT CFILFIYILG TNISIVSYND MQVKHESFFK IAISNMGGDV
NTLNIFTLGL GPWLTSMIIL MLISYRNMDK YMKQTSLEKH YKERILTLIL SVIQSYFVIH
EYVSKERVHQ DNIYLTILIL VTGTMLLVWL ADKNSRYGIA GPMPIVMVSI IKSMMHQKME
YIDASHIVIA LLIILVIITL FILLFIELVE VRIPYIDLMN VSATNMKSYL SWKVNPAGSI
TLMMSISAFV FLKSGIHFIL SMFNKSISDD MPMLTFDSPV GISVYLVIQM LLGYFLSRFL
INTKQKSKDF LKSGNYFSGV KPGKDTERYL NYQARRVCWF GLALVTVIIG IPLYFTLFVP
HLSTEIYFSV QLIVLVYISI NIAETIRTYL YFDKYKPFLN QYW
