SDRE_STAAM
ID SDRE_STAAM Reviewed; 1141 AA.
AC Q932F7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Serine-aspartate repeat-containing protein E;
DE Flags: Precursor;
GN Name=sdrE; OrderedLocusNames=SAV0563;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 270-599, FUNCTION, AND
RP INTERACTION WITH HOST CFAH.
RX PubMed=28258151; DOI=10.1042/bcj20170085;
RA Zhang Y., Wu M., Hang T., Wang C., Yang Y., Pan W., Zang J., Zhang M.,
RA Zhang X.;
RT "Staphylococcus aureus SdrE captures complement factor H's C-terminus via a
RT novel 'close, dock, lock and latch' mechanism for complement evasion.";
RL Biochem. J. 474:1619-1631(2017).
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 (PubMed:28258151). Inhibits
CC also bacterial opsonization and killing by interacting with host
CC complement regulator C4BPA and thus inhibiting classical complement
CC pathway activation (By similarity). {ECO:0000250|UniProtKB:O86489,
CC ECO:0000269|PubMed:28258151}.
CC -!- SUBUNIT: Interacts with host complement factor H/CFAH (via C-terminus)
CC (PubMed:28258151). Interacts with host complement regulator C4BPA (By
CC similarity). {ECO:0000250|UniProtKB:O86489,
CC ECO:0000269|PubMed:28258151}.
CC -!- INTERACTION:
CC Q932F7; P08603: CFH; Xeno; NbExp=4; IntAct=EBI-26369465, EBI-1223708;
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; BA000017; BAB56725.1; -; Genomic_DNA.
DR RefSeq; WP_000610237.1; NC_002758.2.
DR PDB; 5WTA; X-ray; 2.30 A; A/B/C/D=270-599.
DR PDB; 5WTB; X-ray; 3.30 A; A/B/C/D=270-599.
DR PDBsum; 5WTA; -.
DR PDBsum; 5WTB; -.
DR AlphaFoldDB; Q932F7; -.
DR SMR; Q932F7; -.
DR IntAct; Q932F7; 1.
DR MINT; Q932F7; -.
DR PaxDb; Q932F7; -.
DR EnsemblBacteria; BAB56725; BAB56725; SAV0563.
DR KEGG; sav:SAV0563; -.
DR HOGENOM; CLU_004137_1_1_9; -.
DR OMA; VTINKNY; -.
DR PhylomeDB; Q932F7; -.
DR BioCyc; SAUR158878:SAV_RS03140-MON; -.
DR PRO; PR:Q932F7; -.
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; -; 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_0000281165"
FT PROPEP 1108..1141
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281166"
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 929..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 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:5WTA"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:5WTA"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 297..312
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5WTB"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:5WTA"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5WTA"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 376..388
FT /evidence="ECO:0007829|PDB:5WTA"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 427..437
FT /evidence="ECO:0007829|PDB:5WTA"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 456..468
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5WTB"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:5WTA"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5WTA"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 529..537
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 558..568
FT /evidence="ECO:0007829|PDB:5WTA"
FT STRAND 574..585
FT /evidence="ECO:0007829|PDB:5WTA"
SQ SEQUENCE 1141 AA; 124039 MW; E679F7C2991846D9 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 HDDFILDNGY FEEDTSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DAGKHTPVKP MSTTKDHHNK AKALPETGSE NNGSNNATLF GGLFAALGSL LLFGRRKKQN
K
