SECY2_STRSV
ID SECY2_STRSV Reviewed; 407 AA.
AC A3CM55;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=SSA_0832;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(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}.
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DR EMBL; CP000387; ABN44260.1; -; Genomic_DNA.
DR RefSeq; WP_011836742.1; NC_009009.1.
DR RefSeq; YP_001034810.1; NC_009009.1.
DR AlphaFoldDB; A3CM55; -.
DR STRING; 388919.SSA_0832; -.
DR EnsemblBacteria; ABN44260; ABN44260; SSA_0832.
DR KEGG; ssa:SSA_0832; -.
DR PATRIC; fig|388919.9.peg.795; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_4_0_9; -.
DR OMA; YSYLEIM; -.
DR OrthoDB; 1567535at2; -.
DR Proteomes; UP000002148; Chromosome.
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; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..407
FT /note="Accessory Sec system protein translocase subunit
FT SecY2"
FT /id="PRO_0000414212"
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 190..210
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; 46130 MW; FEF60038BC10F7FD CRC64;
MKSFFKPVII KKFLWTLFFL FIYVLGTKLT LPFVDMSKAA AMDGTSTTLN YATALMGGNL
RSMSLFSVGL SPWMSSMLIW QMFAVSKRLG LSKLPLEVQE RRRMLLTLVI ALIQSVALVL
NLPLQEAAGV DMTTIMVLDT LVLMAGTYFL IWLTDLNAAM GLGGSIMIVM ASMIAYIPQD
IWNSIQELKI SSLWLALMLV FSLVFLYLAV TVERSKYRIP VNKINIHNRF KKYSYLDIRL
NPAGGMPIMY AMTLVSIPQY FLLIIHFLQP ENQLIEQWIE ALSMGSPAWF ILYLLTIFIL
ALAFAFINIS GDQIAERMQK SGEYIENVYP GGATRRYING LVTYFALVGA FYLILISGLP
MMVVLVDIRY LRLSMIPGIF MIFIGMVFSI KDEVEALTLN DRYRSLL