ID   SDRD_STAA3              Reviewed;        1381 AA.
AC   Q2FJ78;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Serine-aspartate repeat-containing protein D;
DE   Flags: Precursor;
GN   Name=sdrD; OrderedLocusNames=SAUSA300_0547;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD20874.1; -; Genomic_DNA.
DR   RefSeq; WP_000934424.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FJ78; -.
DR   SMR; Q2FJ78; -.
DR   PRIDE; Q2FJ78; -.
DR   EnsemblBacteria; ABD20874; ABD20874; SAUSA300_0547.
DR   KEGG; saa:SAUSA300_0547; -.
DR   HOGENOM; CLU_004137_0_1_9; -.
DR   OMA; NKTAMTR; -.
DR   PRO; PR:Q2FJ78; -.
DR   Proteomes; UP000001939; 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..1347
FT                   /note="Serine-aspartate repeat-containing protein D"
FT                   /id="PRO_0000281202"
FT   PROPEP          1348..1381
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000281203"
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          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..1357
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           1344..1348
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..1316
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1317..1344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1347
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1381 AA;  149448 MW;  18AA5A7122547DE2 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
     AGLTQTGTNT TEDDKDADGG EVDVTITDHD DFTLDNGYYE EETSDSDSDS DSDSDSDRDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDRDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DAGKHTPVKP MSTTKDHHNK AKALPETGNE NSGSNNATLF GGLFAALGSL LLFGRRKKQN
     K