SDRD_STAAE
ID SDRD_STAAE Reviewed; 1315 AA.
AC O86488; A6QEL4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Serine-aspartate repeat-containing protein D;
DE Flags: Precursor;
GN Name=sdrD; OrderedLocusNames=NWMN_0524;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 CALCIUM-BINDING.
RX PubMed=9813018; DOI=10.1074/jbc.273.47.31145;
RA Josefsson E., O'Connell D., Foster T.J., Durussel I., Cox J.A.;
RT "The binding of calcium to the B-repeat segment of sdrD, a cell surface
RT protein of Staphylococcus aureus.";
RL J. Biol. Chem. 273:31145-31152(1998).
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).
CC -!- FUNCTION: Cell surface-associated calcium-binding protein which plays
CC an important role in adhesion and pathogenesis (PubMed:9884231).
CC Mediates interactions with components of the extracellular matrix such
CC as host DSG1 to promote bacterial adhesion to host cells. Contributes
CC to the resistance to killing by innate immune components such as
CC neutrophils present in blood and thus attenuates bacterial clearance
CC (By similarity). {ECO:0000250|UniProtKB:Q2G0L4,
CC ECO:0000269|PubMed:9884231}.
CC -!- SUBUNIT: Interacts with host DSG1; this interaction increases S. aureus
CC adherence to keratinocytes. {ECO:0000250|UniProtKB:Q2G0L4}.
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 -!- PTM: Anchored to the cell wall by sortase A.
CC {ECO:0000305|PubMed:11830639}.
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; AJ005646; CAA06651.1; -; Genomic_DNA.
DR EMBL; AP009351; BAF66796.1; -; Genomic_DNA.
DR PIR; T28679; T28679.
DR RefSeq; WP_000934419.1; NZ_CP023390.1.
DR AlphaFoldDB; O86488; -.
DR SMR; O86488; -.
DR EnsemblBacteria; BAF66796; BAF66796; NWMN_0524.
DR KEGG; sae:NWMN_0524; -.
DR HOGENOM; CLU_004137_0_1_9; -.
DR OMA; NKTAMTR; -.
DR PRO; PR:O86488; -.
DR Proteomes; UP000006386; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR DisProt; DP00065; -.
DR Gene3D; 2.60.40.10; -; 5.
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; 5.
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.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1281
FT /note="Serine-aspartate repeat-containing protein D"
FT /id="PRO_0000280235"
FT PROPEP 1282..1315
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:11830639"
FT /id="PRO_0000280236"
FT DOMAIN 569..680
FT /note="CNA-B 1"
FT DOMAIN 681..791
FT /note="CNA-B 2"
FT DOMAIN 792..901
FT /note="CNA-B 3"
FT DOMAIN 902..1012
FT /note="CNA-B 4"
FT DOMAIN 1013..1123
FT /note="CNA-B 5"
FT REGION 36..568
FT /note="Ligand binding A region"
FT REGION 54..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1291
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:Q2G0L4"
FT MOTIF 1278..1282
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 54..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1250
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1281
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1315 AA; 142776 MW; 58D4E1F48EE6A689 CRC64;
MLNRENKTAI TRKGMVSNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAESTNKEL
NEATTSASDN QSSDKVDMQQ LNQEDNTKND NQKEMVSSQG NETTSNGNKL IEKESVQSTT
GNKVEVSTAK SDEQASPKST NEDLNTKQTI SNQEALQPDL QENKSVVNVQ PTNEENKKVD
AKTESTTLNV KSDAIKSNDE TLVDNNSNSN NENNADIILP KSTAPKRLNT RMRIAAVQPS
STEAKNVNDL ITSNTTLTVV DADKNNKIVP AQDYLSLKSQ ITVDDKVKSG DYFTIKYSDT
VQVYGLNPED IKNIGDIKDP NNGETIATAK HDTANNLITY TFTDYVDRFN SVQMGINYSI
YMDADTIPVS KNDVEFNVTI GNTTTKTTAN IQYPDYVVNE KNSIGSAFTE TVSHVGNKEN
PGYYKQTIYV NPSENSLTNA KLKVQAYHSS YPNNIGQINK DVTDIKIYQV PKGYTLNKGY
DVNTKELTDV TNQYLQKITY GDNNSAVIDF GNADSAYVVM VNTKFQYTNS ESPTLVQMAT
LSSTGNKSVS TGNALGFTNN QSGGAGQEVY KIGNYVWEDT NKNGVQELGE KGVGNVTVTV
FDNNTNTKVG EAVTKEDGSY LIPNLPNGDY RVEFSNLPKG YEVTPSKQGN NEELDSNGLS
SVITVNGKDN LSADLGIYKP KYNLGDYVWE DTNKNGIQDQ DEKGISGVTV TLKDENGNVL
KTVTTDADGK YKFTDLDNGN YKVEFTTPEG YTPTTVTSGS DIEKDSNGLT TTGVINGADN
MTLDSGFYKT PKYNLGNYVW EDTNKDGKQD STEKGISGVT VTLKNENGEV LQTTKTDKDG
KYQFTGLENG TYKVEFETPS GYTPTQVGSG TDEGIDSNGT STTGVIKDKD NDTIDSGFYK
PTYNLGDYVW EDTNKNGVQD KDEKGISGVT VTLKDENDKV LKTVTTDENG KYQFTDLNNG
TYKVEFETPS GYTPTSVTSG NDTEKDSNGL TTTGVIKDAD NMTLDSGFYK TPKYSLGDYV
WYDSNKDGKQ DSTEKGIKDV KVTLLNEKGE VIGTTKTDEN GKYCFDNLDS GKYKVIFEKP
AGLTQTGTNT TEDDKDADGG EVDVTITDHD DFTLDNGYYE EETSDSDSDS DSDSDSDRDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDRDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDAGKHT
PVKPMSTTKD HHNKAKALPE TGNENSGSNN ATLFGGLFAA LGSLLLFGRR KKQNK
