SDRE_STAA3
ID SDRE_STAA3 Reviewed; 1154 AA.
AC Q2FJ77;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Serine-aspartate repeat-containing protein E;
DE Flags: Precursor;
GN Name=sdrE; OrderedLocusNames=SAUSA300_0548;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD22410.1; -; Genomic_DNA.
DR RefSeq; WP_000610319.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FJ77; -.
DR SMR; Q2FJ77; -.
DR EnsemblBacteria; ABD22410; ABD22410; SAUSA300_0548.
DR KEGG; saa:SAUSA300_0548; -.
DR HOGENOM; CLU_004137_1_1_9; -.
DR OMA; VTINKNY; -.
DR PRO; PR:Q2FJ77; -.
DR Proteomes; UP000001939; 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 3: Inferred from homology;
KW Calcium; Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..1120
FT /note="Serine-aspartate repeat-containing protein E"
FT /id="PRO_0000281161"
FT PROPEP 1121..1154
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281162"
FT DOMAIN 607..719
FT /note="CNA-B 1"
FT DOMAIN 720..829
FT /note="CNA-B 2"
FT DOMAIN 830..940
FT /note="CNA-B 3"
FT REGION 53..606
FT /note="Ligand binding A region"
FT REGION 54..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1129
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 1117..1121
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 154..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..1089
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1120
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1154 AA; 125267 MW; 48C04A9BA508EB28 CRC64;
MINRDNKKAI TKKGMISNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAENTSTEN
AKQDDATTSD NKEVVSETEN NSTTENNSTN PIKKETNTDS QPEAKKESTS SSTQKQQNNV
TATTETKPQN IEKENVKPST DKTATEDTSV ILEEKKAPNN TNNDVTTKPS TSEPSTSEIQ
TKPTTPQEST NIENSQPQPT PSKVDNQVTD ATNPKEPVNV SKEELKNNPE KLKELVRNDS
NTDHSTKPVA TAPTSVAPKR VNAKMRFAVA QPAAVASNNV NDLIKVTKQT IKVGDGKDNV
AAAHDGKDIE YDTEFTIDNK VKKGDTMTIN YDKNVIPSDL TDKNDPIDIT DPSGEVIAKG
TFDKATKQIT YTFTDYVDKY EDIKSRLTLY SYIDKKTVPN ETSLNLTFAT AGKETSQNVT
VDYQDPMVHG DSNIQSIFTK LDEDKQTIEQ QIYVNPLKKS ATNTKVDIAG SQVDDYGNIK
LGNGSTIIDQ NTEIKVYKVN SDQQLPQSNR IYDFSQYEDV TSQFDNKKSF SNNVATLDFG
DINSAYIIKV VSKYTPTSDG ELDIAQGTSM RTTDKYGYYN YAGYSNFIVT SNDTGGGDGT
VKPEEKLYKI GDYVWEDVDK DGVQGTDSKE KPMANVLVTL TYPDGTTKSV RTDANGHYEF
GGLKDGETYT VKFETPTGYL PTKVNGTTDG EKDSNGSSVT VKINGKDDMS LDTGFYKEPK
YNLGDYVWED TNKDGIQDAN EPGIKDVKVT LKDSTGKVIG TTTTDASGKY KFTDLDNGNY
TVEFETPAGY TPTVKNTTAD DKDSNGLTTT GVIKDADNMT LDSGFYKTPK YSLGDYVWYD
SNKDGKQDST EKGIKDVTVT LQNEKGEVIG TTKTDENGKY RFDNLDSGKY KVIFEKPAGL
TQTVTNTTED DKDADGGEVD VTITDHDDFT LDNGYFEEDT SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD SDSDSDSDSD
SDSDSDSDSD SDSDAGKHTP VKPMSTTKDH HNKAKALPET GSENNGSNNA TLFGGLFAAL
GSLLLFGRRK KQNK
