SDRD_STAA8
ID SDRD_STAA8 Reviewed; 1349 AA.
AC Q2G0L4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Serine-aspartate repeat-containing protein D;
DE Flags: Precursor;
GN Name=sdrD; OrderedLocusNames=SAOUHSC_00545;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=RN4220;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=RN4220;
RX PubMed=18800056; DOI=10.1038/emboj.2008.185;
RA DeDent A., Bae T., Missiakas D.M., Schneewind O.;
RT "Signal peptides direct surface proteins to two distinct envelope locations
RT of Staphylococcus aureus.";
RL EMBO J. 27:2656-2668(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROSCOPY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=RN4220;
RX PubMed=20472795; DOI=10.1128/jb.01452-09;
RA Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA van Dijl J.M.;
RT "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT Staphylococcus aureus.";
RL J. Bacteriol. 192:3788-3800(2010).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST DSG1.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=26924733; DOI=10.1038/srep22134;
RA Askarian F., Ajayi C., Hanssen A.M., van Sorge N.M., Pettersen I.,
RA Diep D.B., Sollid J.U., Johannessen M.;
RT "The interaction between Staphylococcus aureus SdrD and desmoglein 1 is
RT important for adhesion to host cells.";
RL Sci. Rep. 6:22134-22134(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NCTC 8325 / PS 47;
RX PubMed=27795358; DOI=10.1128/iai.00559-16;
RA Askarian F., Uchiyama S., Valderrama J.A., Ajayi C., Sollid J.U.E.,
RA van Sorge N.M., Nizet V., van Strijp J.A.G., Johannessen M.;
RT "Serine-Aspartate Repeat Protein D Increases Staphylococcus aureus
RT Virulence and Survival in Blood.";
RL Infect. Immun. 85:0-0(2017).
CC -!- FUNCTION: Cell surface-associated calcium-binding protein which plays
CC an important role in adhesion and pathogenesis (PubMed:26924733).
CC Mediates interactions with components of the extracellular matrix such
CC as host DSG1 to promote bacterial adhesion to host cells
CC (PubMed:26924733). Contributes to the resistance to killing by innate
CC immune components such as neutrophils present in blood and thus
CC attenuates bacterial clearance (PubMed:27795358).
CC {ECO:0000269|PubMed:26924733, ECO:0000269|PubMed:27795358}.
CC -!- SUBUNIT: Interacts with host DSG1; this interaction increases S. aureus
CC adherence to keratinocytes. {ECO:0000269|PubMed:26924733}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:18800056,
CC ECO:0000269|PubMed:20472795, ECO:0000305|PubMed:11830639};
CC Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
CC ECO:0000269|PubMed:20472795, ECO:0000305|PubMed:11830639}. Note=Found
CC in a ring-like distribution on the cell surface (PubMed:18800056).
CC Colocalizes with ClfB (PubMed:18800056). Anchored to the cell wall by
CC sortase A (Probable). {ECO:0000269|PubMed:18800056,
CC ECO:0000305|PubMed:11830639}.
CC -!- INDUCTION: Less protein is secreted in a secG mutant (at protein
CC level). {ECO:0000269|PubMed:20472795}.
CC -!- DISRUPTION PHENOTYPE: About 3.5-fold reduction of survival rate in
CC human blood and about 2-fold reduction in mouse blood.
CC {ECO:0000269|PubMed:27795358}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {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; CP000253; ABD29693.1; -; Genomic_DNA.
DR RefSeq; WP_000934431.1; NZ_LS483365.1.
DR RefSeq; YP_499118.1; NC_007795.1.
DR AlphaFoldDB; Q2G0L4; -.
DR SMR; Q2G0L4; -.
DR STRING; 1280.SAXN108_0618; -.
DR EnsemblBacteria; ABD29693; ABD29693; SAOUHSC_00545.
DR GeneID; 3920825; -.
DR KEGG; sao:SAOUHSC_00545; -.
DR PATRIC; fig|93061.5.peg.491; -.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_004137_0_1_9; -.
DR OMA; NKTAMTR; -.
DR PRO; PR:Q2G0L4; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 5.
DR Gene3D; 2.60.40.1280; -; 1.
DR InterPro; IPR011266; Adhesin_Fg-bd_dom_2.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR033764; Sdr_B.
DR InterPro; IPR041171; SDR_Ig.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF17961; Big_8; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF17210; SdrD_B; 5.
DR Pfam; PF10425; SdrG_C_C; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell wall; Peptidoglycan-anchor; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1315
FT /note="Serine-aspartate repeat-containing protein D"
FT /id="PRO_0000281204"
FT PROPEP 1316..1349
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000281205"
FT DOMAIN 569..680
FT /note="CNA-B 1"
FT DOMAIN 681..791
FT /note="CNA-B 2"
FT DOMAIN 792..901
FT /note="CNA-B 3"
FT DOMAIN 902..1012
FT /note="CNA-B 4"
FT DOMAIN 1013..1123
FT /note="CNA-B 5"
FT REGION 36..568
FT /note="Ligand binding A region"
FT REGION 54..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..34
FT /note="YSIRK-G/S signaling motif"
FT /evidence="ECO:0000305|PubMed:18800056"
FT MOTIF 1312..1316
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 54..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1315
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1349 AA; 146087 MW; B551763296A2C432 CRC64;
MLNRENKTAI TRKGMVSNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAESTNKEL
NEATTSASDN QSSDKVDMQQ LNQEDNTKND NQKEMVSSQG NETTSNGNKL IEKESVQSTT
GNKVEVSTAK SDEQASPKST NEDLNTKQTI SNQEALQPDL QENKSVVNVQ PTNEENKKVD
AKTESTTLNV KSDAIKSNDE TLVDNNSNSN NENNADIILP KSTAPKRLNT RMRIAAVQPS
STEAKNVNDL ITSNTTLTVV DADKNNKIVP AQDYLSLKSQ ITVDDKVKSG DYFTIKYSDT
VQVYGLNPED IKNIGDIKDP NNGETIATAK HDTANNLITY TFTDYVDRFN SVQMGINYSI
YMDADTIPVS KNDVEFNVTI GNTTTKTTAN IQYPDYVVNE KNSIGSAFTE TVSHVGNKEN
PGYYKQTIYV NPSENSLTNA KLKVQAYHSS YPNNIGQINK DVTDIKIYQV PKGYTLNKGY
DVNTKELTDV TNQYLQKITY GDNNSAVIDF GNADSAYVVM VNTKFQYTNS ESPTLVQMAT
LSSTGNKSVS TGNALGFTNN QSGGAGQEVY KIGNYVWEDT NKNGVQELGE KGVGNVTVTV
FDNNTNTKVG EAVTKEDGSY LIPNLPNGDY RVEFSNLPKG YEVTPSKQGN NEELDSNGLS
SVITVNGKDN LSADLGIYKP KYNLGDYVWE DTNKNGIQDQ DEKGISGVTV TLKDENGNVL
KTVTTDADGK YKFTDLDNGN YKVEFTTPEG YTPTTVTSGS DIEKDSNGLT TTGVINGADN
MTLDSGFYKT PKYNLGNYVW EDTNKDGKQD STEKGISGVT VTLKNENGEV LQTTKTDKDG
KYQFTGLENG TYKVEFETPS GYTPTQVGSG TDEGIDSNGT STTGVIKDKD NDTIDSGFYK
PTYNLGDYVW EDTNKNGVQD KDEKGISGVT VTLKDENDKV LKTVTTDENG KYQFTDLNNG
TYKVEFETPS GYTPTSVTSG NDTEKDSNGL TTTGVIKDAD NMTLDSGFYK TPKYSLGDYV
WYDSNKDGKQ DSTEKGIKDV KVTLLNEKGE VIGTTKTDEN GKYCFDNLDS GKYKVIFEKP
AGLTQTVTNT TEDDKDADGG EVDVTITDHD DFTLDNGYFE EDTSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDA GKHTPVKPMS TTKDHHNKAK ALPETGSENN
GSNNATLFGG LFAALGSLLL FGRRKKQNK
