SDRD_STAAM
ID SDRD_STAAM Reviewed; 1385 AA.
AC Q99W47;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine-aspartate repeat-containing protein D;
DE Flags: Precursor;
GN Name=sdrD; OrderedLocusNames=SAV0562;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
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).
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; BA000017; BAB56724.1; -; Genomic_DNA.
DR RefSeq; WP_000934467.1; NC_002758.2.
DR AlphaFoldDB; Q99W47; -.
DR SMR; Q99W47; -.
DR PaxDb; Q99W47; -.
DR EnsemblBacteria; BAB56724; BAB56724; SAV0562.
DR KEGG; sav:SAV0562; -.
DR HOGENOM; CLU_004137_0_1_9; -.
DR OMA; NKTAMTR; -.
DR PhylomeDB; Q99W47; -.
DR BioCyc; SAUR158878:SAV_RS03135-MON; -.
DR PRO; PR:Q99W47; -.
DR Proteomes; UP000002481; 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..1351
FT /note="Serine-aspartate repeat-containing protein D"
FT /id="PRO_0000281208"
FT PROPEP 1352..1385
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281209"
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
