SDRE_STAAC
ID SDRE_STAAC Reviewed; 1166 AA.
AC Q5HIB2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Serine-aspartate repeat-containing protein E;
DE Flags: Precursor;
GN Name=sdrE; OrderedLocusNames=SACOL0610;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37719.1; -; Genomic_DNA.
DR RefSeq; WP_000610303.1; NC_002951.2.
DR AlphaFoldDB; Q5HIB2; -.
DR SMR; Q5HIB2; -.
DR EnsemblBacteria; AAW37719; AAW37719; SACOL0610.
DR KEGG; sac:SACOL0610; -.
DR HOGENOM; CLU_004137_1_1_9; -.
DR OMA; VTINKNY; -.
DR Proteomes; UP000000530; 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..1132
FT /note="Serine-aspartate repeat-containing protein E"
FT /id="PRO_0000281163"
FT PROPEP 1133..1166
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281164"
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..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1141
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 1129..1133
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 217..241
FT /note="Basic and acidic 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..1101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1132
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1166 AA; 126563 MW; 92DFC023B75ABE8F CRC64;
MINRDNKKAI TKKGMISNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAENTSTEN
AKQDDATTSD NKEVVSETEN NSTTENNSTN PIKKETNTDS QPEAKKESTS SSTQKQQNNV
TATTETKPQN IEKENVKPST DKTATEDTSV ILEEKKAPNN TNNDVTTKPS TSEPSTSEIQ
TKPTTPQEST NIENSQPQPT PSKVDNQVTD ATNPKEPVNV SKEELKKNPE 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 LDRGFYKTPK 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 SDSDSDSDSD SDSDSDAGKH TPVKPMSTTK DHHNKAKALP ETGSENNGSN
NATLFGGLFA ALGSLLLFGR RKKQNK
