ID   SDRE_STAAN              Reviewed;        1141 AA.
AC   Q99W46;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Serine-aspartate repeat-containing protein E;
DE   Flags: Precursor;
GN   Name=sdrE; OrderedLocusNames=SA0521;
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. Contributes to the
CC       resistance to killing by innate immune components in blood and thus
CC       attenuates bacterial clearance by interacting with host complement
CC       factor H/CFAH and modulating its activity. Inhibits also bacterial
CC       opsonization and killing by interacting with host complement regulator
CC       C4BPA and thus inhibiting classical complement pathway activation.
CC       {ECO:0000250|UniProtKB:O86489}.
CC   -!- SUBUNIT: Interacts with host complement factor H/CFAH (via C-terminus).
CC       Interacts with host complement regulator C4BPA.
CC       {ECO:0000250|UniProtKB:O86489}.
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:O86489}.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000305}.
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DR   EMBL; BA000018; BAB41752.1; -; Genomic_DNA.
DR   PIR; E89824; E89824.
DR   RefSeq; WP_000610259.1; NC_002745.2.
DR   AlphaFoldDB; Q99W46; -.
DR   SMR; Q99W46; -.
DR   EnsemblBacteria; BAB41752; BAB41752; BAB41752.
DR   KEGG; sau:SA0521; -.
DR   HOGENOM; CLU_004137_1_1_9; -.
DR   OMA; VTINKNY; -.
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; -; 3.
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; 3.
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;
KW   Virulence.
FT   SIGNAL          1..52
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..1107
FT                   /note="Serine-aspartate repeat-containing protein E"
FT                   /id="PRO_0000281167"
FT   PROPEP          1108..1141
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000281168"
FT   DOMAIN          602..714
FT                   /note="CNA-B 1"
FT   DOMAIN          715..824
FT                   /note="CNA-B 2"
FT   DOMAIN          825..935
FT                   /note="CNA-B 3"
FT   REGION          53..601
FT                   /note="Ligand binding A region"
FT   REGION          54..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..1117
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:O86489"
FT   MOTIF           1104..1108
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        73..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..928
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..1076
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1077..1104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1107
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1141 AA;  124027 MW;  445419D0B8C5A4F8 CRC64;
     MINRDNKKAI TKKGMISNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAENTSTEN
     AKQDDATTSD NKEVVSETEN NSTTENDSTN PIKKETNTDS QPEAKEESTT SSTQQQQNNV
     TATTETKPQN IEKENVKPST DKTATEDTSV ILEEKKAPNY TNNDVTTKPS TSEIQTKPTT
     PQESTNIENS QPQPTPSKVD NQVTDATNPK EPVNVSKEEL KNNPEKLKEL VRNDNNTDRS
     TKPVATAPTS VAPKRLNAKM RFAVAQPAAV ASNNVNDLIT VTKQTIKVGD GKDNVAAAHD
     GKDIEYDTEF TIDNKVKKGD TMTINYDKNV IPSDLTDKND PIDITDPSGE VIAKGTFDKA
     TKQITYTFTD YVDKYEDIKA RLTLYSYIDK QAVPNETSLN LTFATAGKET SQNVSVDYQD
     PMVHGDSNIQ SIFTKLDENK QTIEQQIYVN PLKKTATNTK VDIAGSQVDD YGNIKLGNGS
     TIIDQNTEIK VYKVNPNQQL PQSNRIYDFS QYEDVTSQFD NKKSFSNNVA TLDFGDINSA
     YIIKVVSKYT PTSDGELDIA QGTSMRTTDK YGYYNYAGYS NFIVTSNDTG GGDGTVKPEE
     KLYKIGDYVW EDVDKDGVQG TDSKEKPMAN VLVTLTYPDG TTKSVRTDAN GHYEFGGLKD
     GETYTVKFET PAGYLPTKVN GTTDGEKDSN GSSITVKING KDDMSLDTGF YKEPKYNLGD
     YVWEDTNKDG IQDANEPGIK DVKVTLKDST GKVIGTTTTD ASGKYKFTDL DNGNYTVEFE
     TPAGYTPTVK NTTAEDKDSN GLTTTGVIKD ADNMTLDSGF YKTPKYSLGD YVWYDSNKDG
     KQDSTEKGIK DVKVTLLNEK GEVIGTTKTD ENGKYRFDNL DSGKYKVIFE KPAGLTQTVT
     NTTEDDKDAD GGEVDVTITD HDDFTLDNGY FEEDTSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DAGKHTPVKP MSTTKDHHNK AKALPETGSE NNGSNNATLF GGLFAALGSL LLFGRRKKQN
     K