SDRE_STAAE
ID SDRE_STAAE Reviewed; 1166 AA.
AC O86489; A6QEL5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Serine-aspartate repeat-containing protein E;
DE Flags: Precursor;
GN Name=sdrE; OrderedLocusNames=NWMN_0525;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9884231; DOI=10.1099/00221287-144-12-3387;
RA Josefsson E., McCrea K.W., Eidhin D.N., O'Connell D., Cox J.A., Hoeoek M.,
RA Foster T.J.;
RT "Three new members of the serine-aspartate repeat protein multigene family
RT of Staphylococcus aureus.";
RL Microbiology 144:3387-3395(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=12010496; DOI=10.1046/j.1365-2958.2002.02935.x;
RA O'Brien L.M., Kerrigan S.W., Kaw G., Hogan M., Penades J., Litt D.,
RA Fitzgerald D.J., Foster T.J., Cox D.;
RT "Multiple mechanisms for the activation of human platelet aggregation by
RT Staphylococcus aureus: roles for the clumping factors clfA and clfB, the
RT serine-aspartate repeat protein sdrE and protein A.";
RL Mol. Microbiol. 44:1033-1044(2002).
RN [4]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SORTASE A.
RC STRAIN=Newman;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
RN [5]
RP POTENTIAL USE AS A VACCINE.
RX PubMed=17075065; DOI=10.1073/pnas.0606863103;
RA Stranger-Jones Y.K., Bae T., Schneewind O.;
RT "Vaccine assembly from surface proteins of Staphylococcus aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16942-16947(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST CFAH.
RX PubMed=22675461; DOI=10.1371/journal.pone.0038407;
RA Sharp J.A., Echague C.G., Hair P.S., Ward M.D., Nyalwidhe J.O.,
RA Geoghegan J.A., Foster T.J., Cunnion K.M.;
RT "Staphylococcus aureus surface protein SdrE binds complement regulator
RT factor H as an immune evasion tactic.";
RL PLoS ONE 7:E38407-E38407(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST C4BPA.
RX PubMed=24600566; DOI=10.1016/j.rinim.2013.10.004;
RA Hair P.S., Foley C.K., Krishna N.K., Nyalwidhe J.O., Geoghegan J.A.,
RA Foster T.J., Cunnion K.M.;
RT "Complement regulator C4BP binds to Staphylococcus aureus surface proteins
RT SdrE and Bbp inhibiting bacterial opsonization and killing.";
RL Results Immunol. 3:114-121(2013).
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:22675461). Inhibits
CC also bacterial opsonization and killing by interacting with host
CC complement regulator C4BPA and thus inhibiting classical complement
CC pathway activation (PubMed:24600566). {ECO:0000269|PubMed:22675461,
CC ECO:0000269|PubMed:24600566}.
CC -!- SUBUNIT: Interacts with host complement factor H/CFAH (via C-terminus)
CC (PubMed:22675461). Interacts with host complement regulator C4BPA
CC (PubMed:24600566). {ECO:0000269|PubMed:22675461,
CC ECO:0000269|PubMed:24600566}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}.
CC Note=Anchored to the cell wall by sortase A.
CC {ECO:0000305|PubMed:11830639}.
CC -!- INDUCTION: Expressed at both exponential and stationary phases.
CC {ECO:0000269|PubMed:12010496}.
CC -!- BIOTECHNOLOGY: A combined vaccine containing IsdA, IsdB, SdrD and SdrE
CC afforded significant protection in mice against a lethal challenge with
CC S.aureus Newman or any of the clinical isolates NRS252, N315, NRS248,
CC USA100 and USA400. The immune response elicited by the combined vaccine
CC is greater than the one elicited by its individual components.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; AJ005647; CAA06652.1; -; Genomic_DNA.
DR EMBL; AP009351; BAF66797.1; -; Genomic_DNA.
DR PIR; T28680; T28680.
DR RefSeq; WP_000610306.1; NZ_CP023390.1.
DR AlphaFoldDB; O86489; -.
DR SMR; O86489; -.
DR EnsemblBacteria; BAF66797; BAF66797; NWMN_0525.
DR KEGG; sae:NWMN_0525; -.
DR HOGENOM; CLU_004137_1_1_9; -.
DR OMA; VTINKNY; -.
DR PRO; PR:O86489; -.
DR Proteomes; UP000006386; 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..1132
FT /note="Serine-aspartate repeat-containing protein E"
FT /id="PRO_0000280237"
FT PROPEP 1133..1166
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000280238"
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..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:0000305"
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 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; 126549 MW; 750A7B0135287D4A 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 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
