SECY2_STAAB
ID SECY2_STAAB Reviewed; 403 AA.
AC Q2YZ90;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 25-MAY-2022, entry version 88.
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}; OrderedLocusNames=SAB2528c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
CC -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC required for export of possible cell wall proteins. The central subunit
CC of a protein translocation channel. {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- SUBUNIT: Component of the accessory SecA2/SecY2 protein translocase
CC complex required to export cell wall proteins. May form heterotrimers
CC with SecE and SecG subunits. {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01466};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01466}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI82216.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ938182; CAI82216.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q2YZ90; -.
DR KEGG; sab:SAB2528c; -.
DR HOGENOM; CLU_030313_4_0_9; -.
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..403
FT /note="Accessory Sec system protein translocase subunit
FT SecY2"
FT /id="PRO_0000414865"
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 362..382
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
SQ SEQUENCE 403 AA; 46851 MW; 9C97135F345D641E CRC64;
MLKLLQQYEY KIIYKRILYT CFILFIYILG SNISIVSYND MQVKHESFFK IAISNMGGDV
NTLNIFTLGL GPWLTSMIIL MLISYRNMDK YMKQTSLEKH YKERILTLIL SVIQSYFVIH
EYVSKQRVHQ DNIYLTILIL VTGTMLLVWL ADKNSRYGIA GPMPIVMVSI IKSMMHQKME
YIDASHIVIA LLIILVIITL FILLFIELVE VRIPYIDLMN VSATNMKSYL SWKVNPAGSI
TLMMSISAFV FLKSGIHFIL SIFNKSISDD MPMLKFDSPV GISVYLVIQM LLGYFLSRFL
INTKQKSKDF LKSGNYFSGV KPGKDTERYL NYQARRVCWF GSALVTIIIG IPLYFTLFVP
HLSIEIYFSV QLIVLVYISI NIAETIRTYL YFDKYKSFLN QYW