SECY2_STAPE
ID SECY2_STAPE Reviewed; 407 AA.
AC F0P5S5;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 51.
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=SPSE_0165;
OS Staphylococcus pseudintermedius (strain ED99).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus; Staphylococcus intermedius group.
OX NCBI_TaxID=984892;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED99;
RX PubMed=21398539; DOI=10.1128/jb.00137-11;
RA Zakour N.L., Bannoehr J., van den Broek A.H., Thoday K.L., Fitzgerald J.R.;
RT "Complete genome sequence of the canine pathogen Staphylococcus
RT pseudintermedius.";
RL J. Bacteriol. 193:2363-2364(2011).
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}.
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DR EMBL; CP002478; ADX75512.1; -; Genomic_DNA.
DR AlphaFoldDB; F0P5S5; -.
DR SMR; F0P5S5; -.
DR KEGG; sdt:SPSE_0165; -.
DR PATRIC; fig|984892.3.peg.156; -.
DR HOGENOM; CLU_030313_4_0_9; -.
DR OMA; LAMNITE; -.
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_0000414872"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01466"
FT TRANSMEM 343..363
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 407 AA; 46804 MW; 9AF9CE755D8511C8 CRC64;
MKNNRITKII NQYEYKIFYK RIAFTILILL IYILGSKITI VDENAMRQHD SAFYKLAVSN
MGGDIHQLNV FSLGLGPWLT AMIIISLITY KNMEKAMHQT RAEKHYKEKF LTLGLSIIQG
YFVINQFVRH TDAKRFTELL LLLILVTGAM LMMWLADQNM RYGIAGPMPI VLLSVIKSMF
TQSLPIVSIE ILMLVVMVIL IIVALFILLL TELIEYRIHY RDIIEMPTPG QPTYLAWKIN
PGGSISIMIS LSVFLLLTST INLIFNMVTG KTPHLQWLSF GHYMGVTIYL ILQTVLGYLL
SRLIVNTKQN TKDFLKNGNY FIGIRPGADT GNYLNHLAKR LCWFGTTIVT AIIGVPLYIS
LLVPDLSEYI YFAVQLMIMV YLAMNITETM RTYLYFDKYG AFLNQYW