ID   SDRE_STAAS              Reviewed;        1141 AA.
AC   Q6GBS4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Serine-aspartate repeat-containing protein E;
DE   Flags: Precursor;
GN   Name=sdrE; OrderedLocusNames=SAS0521;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG42296.1; -; Genomic_DNA.
DR   RefSeq; WP_000610231.1; NC_002953.3.
DR   PDB; 5IHW; X-ray; 1.25 A; A=273-586.
DR   PDBsum; 5IHW; -.
DR   AlphaFoldDB; Q6GBS4; -.
DR   SMR; Q6GBS4; -.
DR   KEGG; sas:SAS0521; -.
DR   HOGENOM; CLU_004137_1_1_9; -.
DR   OMA; VTINKNY; -.
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   3D-structure; Calcium; Cell wall; Peptidoglycan-anchor; Repeat; Secreted;
KW   Signal; Virulence.
FT   SIGNAL          1..52
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..1107
FT                   /note="Serine-aspartate repeat-containing protein E"
FT                   /id="PRO_0000281171"
FT   PROPEP          1108..1141
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000281172"
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..225
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..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..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        154..211
FT                   /note="Polar 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"
FT   HELIX           276..278
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          279..290
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          297..312
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          321..325
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          351..358
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   TURN            359..362
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          363..368
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   HELIX           371..374
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          376..388
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   TURN            390..392
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          397..405
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          408..416
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          422..424
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          427..437
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   TURN            438..441
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          442..450
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          456..468
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          474..480
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          487..493
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   HELIX           509..511
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          512..514
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   HELIX           516..519
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          522..526
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          529..537
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          541..548
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          558..568
FT                   /evidence="ECO:0007829|PDB:5IHW"
FT   STRAND          574..585
FT                   /evidence="ECO:0007829|PDB:5IHW"
SQ   SEQUENCE   1141 AA;  123998 MW;  372E5860850A332C CRC64;
     MINRDNKKAI TKKGMISNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAENTSTEN
     AKQDDATTSD NKEVVSEAEN NSTTENDSTN PIKKETNTDS QPEAKEESTK SSTQQQQNNV
     TATTETKPQN IEKENVKPST DKTATEDTSV ILEEKKAPNN TNNDVTTKPS TSEIQTKPTT
     PQESTNIENS QPQPTPSKVD NQVTDATNPK EPVNVSKEEL KNNPEKLKEL VRNDSNTDHS
     TKPVATAPTS VAPKRVNAKM RFAVAQPAAV ASNNVNDLIK VTKQTIKVGD GKDNVAAAHD
     GKDIEYDTEF TIDNKVKKGD TMTINYDKNV IPSDLTDKND PIDITDPSGE VIAKGTFDKA
     TKQITYTFTD YVDKYEDIKS RLTLYSYIDK KTVPNETSLN LTFATAGKET SQNVTVDYQD
     PMVHGDSNIQ SIFTKLDEDK QTIEQQIYVN PLKKSATNTK VDIAGSQVDD YGNIKLGNGS
     TIIDQNTEIK VYKVNSDQQL PQSNRIYDFS QYEDVTSQFD NKKSFSNNVA TLDFGDINSA
     YIIKVVSKYT PTSDGELDIA QGTSMRTTDK YGYYNYAGYS NFIVTSNDSG GGDGTVKPEE
     KLYKIGDYVW EDVDKDGVQG TDSKEKPMAN VLVTLTYPDG TTKSVRTDAK GHYEFGGLKD
     GETYTVKFET PTGYLPTKVN GTTDGEKDSN GSSVTVKING KDDMSLDTGF YKEPKYNLGD
     YVWEDTNKDG IQDANEPGIK DVKVTLKDST GKVIGTTTTD ASGKYKFTDL DNGNYTVEFE
     TPAGYTPTVK NTTAEDKDSN GLTTTGVIKD ADNMTLDSGF YKTPKYSLGD YVWYDSNKDG
     KQDSTEKGIK DVTVTLQNEK GEVIGTTKTD ENGKYRFDNL DSGKYKVIFE KPAGLTQTVT
     NTTEDDKDAD GGEVDVTITD HDDFTLDNGY FEEDTSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSESDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
     DAGKHTPVKP MSTTKDHHNK AKALPETGSE NNGSNNATLF GGLFAALGSL LLFGRRKKQN
     K