ID   ASP2_STRGN              Reviewed;         510 AA.
AC   Q9AET8;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Accessory Sec system protein Asp2;
DE   AltName: Full=Accessory secretory protein Asp2;
DE   AltName: Full=Orf2;
GN   Name=asp2;
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
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       Q9AET8; Q939N5: gspB; NbExp=4; IntAct=EBI-6414583, EBI-6414561;
CC   -!- DISRUPTION PHENOTYPE: Loss of export of cell wall protein GspB, the
CC       protein accumulates intracellularly in protoplasts.
CC       {ECO:0000269|PubMed:12010500, ECO:0000269|PubMed:15049820}.
CC   -!- SIMILARITY: Belongs to the accessory Sec system protein Asp2 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY028381; AAK16999.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AET8; -.
DR   SMR; Q9AET8; -.
DR   IntAct; Q9AET8; 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; IPR029058; AB_hydrolase.
DR   InterPro; IPR022267; Asp2.
DR   Pfam; PF16929; Asp2; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03712; acc_sec_asp2; 1.
PE   1: Evidence at protein level;
KW   Protein transport; Translocation; Transport.
FT   CHAIN           1..510
FT                   /note="Accessory Sec system protein Asp2"
FT                   /id="PRO_0000414198"
SQ   SEQUENCE   510 AA;  59205 MW;  54014EE4F575EE08 CRC64;
     MKNKLKILQI GSIDWSKEVV IPDNMDWYYF FSLTLRLAIK KVMEMEKINH FSAIIVDDLD
     LIPDLFLIES RIIPYTIFYS KKQQAIQEPI AFFLKRYCAQ QIDLSDRPNL LRKLSKALFR
     GQYGDKMTPL DMVVSPGFKG RICHNGYENL ELEGNFGSDF RPIVSWKYNI VASKKNPVEI
     WLEYEKDLSC ELRLRIYNIQ EGSAADLVRE SVFSETDMEE TIVLDNDFTS FLGITLEARG
     FGTLKIGAFH QRLTRYQFGK FVLGGKILKD SHRQEINYFF YPGDFKPPLV VYFSGYRRAE
     GFEGFGMMRG LGCPFLLISD QRLDGGVFYL GSDELEEGIR RIIQEHMELL GFSERELILS
     GISMGTYGAA YYGADFSPRA IILCKPLANL GTIAQRGRLR LPEVFPMALD ILHRHTGGKD
     RENVMELDNR YWKKFKKADF SRTIFGLAYM KEEDYDPTAY EDLVQYLYPT ETQLMSNGLS
     GRHNDDSTMV INWFMNYHRI ILEKEFGRKK