ID   SDRD_STAAW              Reviewed;        1347 AA.
AC   Q8NXX6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Serine-aspartate repeat-containing protein D;
DE   Flags: Precursor;
GN   Name=sdrD; OrderedLocusNames=MW0517;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Cell surface-associated calcium-binding protein which plays
CC       an important role in adhesion and pathogenesis. Mediates interactions
CC       with components of the extracellular matrix such as host DSG1 to
CC       promote bacterial adhesion to host cells. Contributes to the resistance
CC       to killing by innate immune components such as neutrophils present in
CC       blood and thus attenuates bacterial clearance.
CC       {ECO:0000250|UniProtKB:Q2G0L4}.
CC   -!- SUBUNIT: Interacts with host DSG1; this interaction increases S. aureus
CC       adherence to keratinocytes. {ECO:0000250|UniProtKB:Q2G0L4}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}. Note=Anchored to the cell wall by sortase A (By
CC       similarity). {ECO:0000250|UniProtKB:Q2G0L4}.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB94382.1; -; Genomic_DNA.
DR   RefSeq; WP_000934435.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXX6; -.
DR   SMR; Q8NXX6; -.
DR   EnsemblBacteria; BAB94382; BAB94382; BAB94382.
DR   KEGG; sam:MW0517; -.
DR   HOGENOM; CLU_004137_0_1_9; -.
DR   OMA; NKTAMTR; -.
DR   PRO; PR:Q8NXX6; -.
DR   Proteomes; UP000000418; 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   3: Inferred from homology;
KW   Calcium; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..1313
FT                   /note="Serine-aspartate repeat-containing protein D"
FT                   /id="PRO_0000281214"
FT   PROPEP          1314..1347
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000281215"
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          55..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..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          1078..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           23..34
FT                   /note="YSIRK-G/S signaling motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q2G0L4"
FT   MOTIF           1310..1314
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        55..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..1282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1283..1310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1313
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1347 AA;  145960 MW;  AB8D393884AD8034 CRC64;
     MLNRENKTAI TRKGMVSNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAESTNKEL
     NEATTSASDN QSSDKVDMQQ LNQEDNTKND NQKEMVSSQG NETTSNGNKS IEKESVQSTT
     GNKVEVSTAK SDEQASPKST NEDLNTKQTI SNQEALQPDL QENKSVVNAQ PTNEENKKVD
     AKTESTTLNV KSDAIKSNAE TLVDNNSNSN NENNADIILP KSTAPKRLNT RMRIAAVQPS
     STEAKNVNDL ITSNTTLTVV DADKNNKIVP AQDYLELKSQ IKVDDKVKSG DYFTIKYSDT
     VQVYGLNPED IKNIGDIKDP NNGETIATAK HDTANNLITY TFTDYVDRFN SVQMGINYSI
     YMDADTIPVS KNDVEFNVTI GNTTTKTTAN IQYPDYVVNE KNSIGSAFTE TVSHVGNKEN
     PGYYKQTIYI NPSENSLTNA KLKVQAYHSS YPNNIGQINK EVTDIKIYQV PKGYTLNKGY
     DVNTKELTDV TNQYLQKITY GDNNSAVIDF GNADSAYVVM VNTKFQYTTS ESPTLVQMVT
     LSSDNSKSAS MGNALGFTNN 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 TSKYSLGDYV
     WYDSNKDGKQ DSTEKGIKDV KVTLLNEKGE VIGTTKTDEN GKYRFDNLDS GKYKVIFEKP
     AGLTQTGTNT TEDDKDADGG EVDVTITDHD DFTLDNGYFE EDTSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS ESDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDAGK HTPVKPMSTT KDHHNKAKAL PETGNENSGS
     NNATLFGGLF AALGSLLLFG RRKKQNK