ID   ASP3_STRGN              Reviewed;         159 AA.
AC   Q9AET7;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Accessory Sec system protein Asp3;
DE   AltName: Full=Accessory secretory protein Asp3;
DE   AltName: Full=Orf3;
GN   Name=asp3;
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=15049820; DOI=10.1111/j.1365-2958.2004.03978.x;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Genes in the accessory sec locus of Streptococcus gordonii have three
RT   functionally distinct effects on the expression of the platelet-binding
RT   protein GspB.";
RL   Mol. Microbiol. 52:189-203(2004).
RN   [3]
RP   INTERACTION WITH GSPB.
RX   PubMed=21531800; DOI=10.1128/jb.00057-11;
RA   Yen Y.T., Seepersaud R., Bensing B.A., Sullam P.M.;
RT   "Asp2 and Asp3 interact directly with GspB, the export substrate of the
RT   Streptococcus gordonii accessory Sec System.";
RL   J. Bacteriol. 193:3165-3174(2011).
CC   -!- FUNCTION: 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:15049820}.
CC   -!- SUBUNIT: Part of the accessory SecA2/SecY2 protein translocation
CC       apparatus required to export cell wall protein GspB. Binds the Ser-rich
CC       domains (SSR1 and SSR2) of non-glycosylated GspB, binds much less to
CC       glycosylated protein.
CC   -!- INTERACTION:
CC       Q9AET7; Q939N5: gspB; NbExp=4; IntAct=EBI-6414568, EBI-6414561;
CC   -!- DISRUPTION PHENOTYPE: Loss of export of cell wall protein GspB, the
CC       protein accumulates intracellularly in protoplasts.
CC       {ECO:0000269|PubMed:15049820}.
CC   -!- SIMILARITY: Belongs to the accessory Sec system protein Asp3 family.
CC       {ECO:0000305}.
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DR   EMBL; AY028381; AAK17000.1; -; Genomic_DNA.
DR   RefSeq; WP_061598994.1; NZ_LAWL01000014.1.
DR   PDB; 5VAE; X-ray; 3.11 A; B/D/F/H=1-159.
DR   PDBsum; 5VAE; -.
DR   AlphaFoldDB; Q9AET7; -.
DR   SMR; Q9AET7; -.
DR   IntAct; Q9AET7; 1.
DR   TCDB; 3.A.5.10.1; the general secretory pathway (sec) family.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR022259; Acessory_Sec_prot_Asp3.
DR   Pfam; PF15432; Sec-ASP3; 1.
DR   TIGRFAMs; TIGR03711; acc_sec_asp3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Protein transport; Translocation; Transport.
FT   CHAIN           1..159
FT                   /note="Accessory Sec system protein Asp3"
FT                   /id="PRO_0000414200"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          55..61
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          81..90
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          109..123
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:5VAE"
FT   STRAND          142..152
FT                   /evidence="ECO:0007829|PDB:5VAE"
SQ   SEQUENCE   159 AA;  18762 MW;  3E9E8AF9255337DA CRC64;
     MKIQKHKEIY WGELRGASIS KTRKDFTYLY GSTIIFHSPD QVYFENKLIA SGQTIHEWSS
     SWNYQGDRQV PSLPLLKRGR SYSLTRDMTS YPSESVFLKL IFFDRYNREV SNHVERSDKM
     TFTYPEEAYS YKVQLLSAGV ESFEFHCLRI EEILEESNG