ID   ASP5_STRGN              Reviewed;          73 AA.
AC   Q4L2X2;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Accessory secretory protein Asp5;
DE   AltName: Full=Orf6;
DE   Flags: Precursor;
GN   Name=asp5;
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M99;
RX   PubMed=15901716; DOI=10.1128/jb.187.11.3878-3883.2005;
RA   Takamatsu D., Bensing B.A., Sullam P.M.;
RT   "Two additional components of the accessory sec system mediating export of
RT   the Streptococcus gordonii platelet-binding protein GspB.";
RL   J. Bacteriol. 187:3878-3883(2005).
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:15901716}.
CC   -!- SUBUNIT: Part of the accessory SecA2/SecY2 protein translocation
CC       apparatus required to export cell wall protein GspB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: No export of mature cell wall protein GspB, a
CC       small amount of unprocessed protein is exported to the cell wall while
CC       the rest accumulates intracellularly, probably in a glycosylated form.
CC       Cells bind less well to platelets. {ECO:0000269|PubMed:15901716}.
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DR   EMBL; AY028381; AAY99444.1; -; Genomic_DNA.
DR   RefSeq; WP_045634941.1; NZ_RJVY01000036.1.
DR   AlphaFoldDB; Q4L2X2; -.
DR   SMR; Q4L2X2; -.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR031548; Asp5.
DR   Pfam; PF17000; Asp5; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Signal; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..73
FT                   /note="Accessory secretory protein Asp5"
FT                   /id="PRO_0000414202"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   73 AA;  8492 MW;  FF7E9D09C2622484 CRC64;
     MQKLLLILTI LLALILITLV ISLPRENQQF FSETRSTIGK SGYWETNFFK KIILLIVSIL
     LFLTLIFYMI QTA