ID   SDRD_STAAN              Reviewed;        1385 AA.
AC   Q7A780;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Serine-aspartate repeat-containing protein D;
DE   Flags: Precursor;
GN   Name=sdrD; OrderedLocusNames=SA0520;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB41751.1; -; Genomic_DNA.
DR   PIR; D89824; D89824.
DR   RefSeq; WP_000934467.1; NC_002745.2.
DR   AlphaFoldDB; Q7A780; -.
DR   SMR; Q7A780; -.
DR   EnsemblBacteria; BAB41751; BAB41751; BAB41751.
DR   KEGG; sau:SA0520; -.
DR   HOGENOM; CLU_004137_0_1_9; -.
DR   OMA; NKTAMTR; -.
DR   PRO; PR:Q7A780; -.
DR   Proteomes; UP000000751; 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; Repeat; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..1351
FT                   /note="Serine-aspartate repeat-containing protein D"
FT                   /id="PRO_0000281210"
FT   PROPEP          1352..1385
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000281211"
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..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          856..886
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          1077..1361
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           1348..1352
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        1091..1116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1320
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1351
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1385 AA;  149644 MW;  2A0CD277733B3C1D CRC64;
     MLNRENKTAI TRKGMVSNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAESTNKEL
     NEATTSASDN QSSDKVDMQQ LNQEDNTKND NQKEMVSSQG NETTSNGNKS IEKESVQSTT
     GNKVEVSTAK SDEQASPKST NEDLNTKQTI SNQEGLQPDL LENKSVVNVQ PTNEENKKVD
     AKTESTTLNV KSDAIKSNAE TLVDNNSNSN NENNADIILP KSTAPKSLNT RMRMAAIQPN
     STDSKNVNDL ITSNTTLTVV DADNSKTIVP AQDYLSLKSQ ITVDDKVKSG DYFTIKYSDT
     VQVYGLNPED IKNIGDIKDP NNGETIATAK HDTANNLITY TFTDYVDRFN SVKMGINYSI
     YMDADTIPVD KKDVPFSVTI GNQITTTTAD ITYPAYKEAD NNSIGSAFTE TVSHVGNVED
     PGYYNQVVYV NPMDKDLKGA KLKVEAYHPK YPTNIGQINQ NVTNIKIYRV PEGYTLNKGY
     DVNTNDLVDV TDEFKNKMTY GSNQSVNLDF GDITSAYVVM 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 KVILLNEKGE VIGTTKTDEN GKYRFDNLDS GKYKVIFEKP
     TGLTQTGTNT TEDDKDADGG EVDVTITDHD DFTLDNGYYE EETSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDAGKHT PVKPMSTTKD HHNKAKALPE TGNENSGSNN ATLFGGLFAA LGSLLLFGRR
     KKQNK