SDRG_STAEP
ID SDRG_STAEP Reviewed; 931 AA.
AC Q9KI13;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Serine-aspartate repeat-containing protein G;
DE Flags: Precursor;
GN Name=sdrG;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K28;
RX PubMed=10878118; DOI=10.1099/00221287-146-7-1535;
RA McCrea K.W., Hartford O., Davis S., Eidhin D.N., Lina G., Speziale P.,
RA Foster T.J., Hoeoek M.;
RT "The serine-aspartate repeat (Sdr) protein family in Staphylococcus
RT epidermidis.";
RL Microbiology 146:1535-1546(2000).
RN [2]
RP FUNCTION.
RC STRAIN=K28;
RX PubMed=11371571; DOI=10.1074/jbc.m103873200;
RA Davis S.L., Gurusiddappa S., McCrea K.W., Perkins S., Hoeoek M.;
RT "SdrG, a fibrinogen-binding bacterial adhesin of the microbial surface
RT components recognizing adhesive matrix molecules subfamily from
RT Staphylococcus epidermidis, targets the thrombin cleavage site in the Bbeta
RT chain.";
RL J. Biol. Chem. 276:27799-27805(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 274-598 OF APOPROTEIN AND OF
RP COMPLEX WITH HUMAN FIBRINOGEN BETA AND CALCIUM ION, AND MUTAGENESIS OF
RP SER-338 AND ASP-339.
RX PubMed=14567919; DOI=10.1016/s0092-8674(03)00809-2;
RA Ponnuraj K., Bowden M.G., Davis S., Gurusiddappa S., Moore D., Choe D.,
RA Xu Y., Hoeoek M., Narayana S.V.L.;
RT "A 'dock, lock, and latch' structural model for a staphylococcal adhesin
RT binding to fibrinogen.";
RL Cell 115:217-228(2003).
CC -!- FUNCTION: Binds to the N-terminus of the B beta-chain of human
CC fibrinogen and thereby interferes with thrombin cleavage and release of
CC fibrinopeptide B, thus interfering with fibrin clot formation. This may
CC hinder host defense against microbial infections.
CC {ECO:0000269|PubMed:11371571}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; AF245042; AAF72510.1; -; Genomic_DNA.
DR PDB; 1R17; X-ray; 1.86 A; A/B=274-598.
DR PDB; 1R19; X-ray; 3.51 A; A/B/C/D=274-598.
DR PDB; 2RAL; X-ray; 2.80 A; A/B=274-595.
DR PDBsum; 1R17; -.
DR PDBsum; 1R19; -.
DR PDBsum; 2RAL; -.
DR AlphaFoldDB; Q9KI13; -.
DR SMR; Q9KI13; -.
DR EvolutionaryTrace; Q9KI13; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
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; 2.
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; Metal-binding; Peptidoglycan-anchor;
KW Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..50
FT /evidence="ECO:0000255"
FT CHAIN 51..895
FT /note="Serine-aspartate repeat-containing protein G"
FT /id="PRO_0000294172"
FT PROPEP 896..931
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000294173"
FT DOMAIN 598..711
FT /note="CNA-B 1"
FT DOMAIN 712..822
FT /note="CNA-B 2"
FT REGION 51..597
FT /note="Ligand binding A region"
FT REGION 52..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..588
FT /note="Interaction with human fibrinogen"
FT REGION 776..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 892..896
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 52..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..878
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14567919,
FT ECO:0007744|PDB:1R17"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14567919,
FT ECO:0007744|PDB:1R17"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14567919,
FT ECO:0007744|PDB:1R17"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:14567919,
FT ECO:0007744|PDB:1R17"
FT MOD_RES 895
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 338
FT /note="S->H: Loss of interaction with human fibrinogen."
FT /evidence="ECO:0000269|PubMed:14567919"
FT MUTAGEN 339
FT /note="D->A: Loss of interaction with human fibrinogen."
FT /evidence="ECO:0000269|PubMed:14567919"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1R17"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2RAL"
FT STRAND 309..317
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:1R17"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:1R17"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:1R17"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 414..423
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:1R17"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 462..472
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:2RAL"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:1R17"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:1R17"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 522..533
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 537..544
FT /evidence="ECO:0007829|PDB:1R17"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 556..565
FT /evidence="ECO:0007829|PDB:1R17"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 572..584
FT /evidence="ECO:0007829|PDB:1R17"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:1R17"
SQ SEQUENCE 931 AA; 102956 MW; 591E657D97027116 CRC64;
MIKKNNLLTK KKPIANKSNK YAIRKFTVGT ASIVIGAALL FGLGHNEAKA EENTVQDVKD
SNMDDELSDS NDQSSNEEKN DVINNSQSIN TDDDNQIKKE ETNSNDAIEN RSKDITQSTT
NVDENEATFL QKTPQDNTQL KEEVVKEPSS VESSNSSMDT AQQPSHTTIN SEASIQTSDN
EENSRVSDFA NSKIIESNTE SNKEENTIEQ PNKVREDSIT SQPSSYKNID EKISNQDELL
NLPINEYENK VRPLSTTSAQ PSSKRVTVNQ LAAEQGSNVN HLIKVTDQSI TEGYDDSDGI
IKAHDAENLI YDVTFEVDDK VKSGDTMTVN IDKNTVPSDL TDSFAIPKIK DNSGEIIATG
TYDNTNKQIT YTFTDYVDKY ENIKAHLKLT SYIDKSKVPN NNTKLDVEYK TALSSVNKTI
TVEYQKPNEN RTANLQSMFT NIDTKNHTVE QTIYINPLRY SAKETNVNIS GNGDEGSTII
DDSTIIKVYK VGDNQNLPDS NRIYDYSEYE DVTNDDYAQL GNNNDVNINF GNIDSPYIIK
VISKYDPNKD DYTTIQQTVT MQTTINEYTG EFRTASYDNT IAFSTSSGQG QGDLPPEKTY
KIGDYVWEDV DKDGIQNTND NEKPLSNVLV TLTYPDGTSK SVRTDEEGKY QFDGLKNGLT
YKITFETPEG YTPTLKHSGT NPALDSEGNS VWVTINGQDD MTIDSGFYQT PKYSLGNYVW
YDTNKDGIQG DDEKGISGVK VTLKDENGNI ISTTTTDENG KYQFDNLNSG NYIVHFDKPS
GMTQTTTDSG DDDEQDADGE EVHVTITDHD DFSIDNGYYD DDSDSDSDSD SDSDDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSGL DNSSDKNTKD KLPDTGANED
HDSKGTLLGA LFAGLGALLL GKRRKNRKNK N
