SDRF_STAEP
ID SDRF_STAEP Reviewed; 1733 AA.
AC Q9KI14;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Serine-aspartate repeat-containing protein F;
DE Flags: Precursor;
GN Name=sdrF;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9491;
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 IN COLLAGEN BINDING.
RC STRAIN=ATCC 9491;
RX PubMed=17472965; DOI=10.1074/jbc.m610940200;
RA Arrecubieta C., Lee M.-H., Macey A., Foster T.J., Lowy F.D.;
RT "SdrF, a Staphylococcus epidermidis surface protein, binds type I
RT collagen.";
RL J. Biol. Chem. 282:18767-18776(2007).
CC -!- FUNCTION: Binds to type I collagen via alpha-2(I) or alpha-1(I) chains,
CC although its affinity for the alpha-1(I) chain is significantly higher.
CC Involved in bacterial adherence to transcutaneous drivelines from
CC explanted ventricular assist devices. {ECO:0000269|PubMed:17472965}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- DOMAIN: Each CNA-B domain is able to independently mediate adherence to
CC the substrate.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; AF245041; AAF72509.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KI14; -.
DR SMR; Q9KI14; -.
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; -; 4.
DR Gene3D; 2.60.40.1280; -; 1.
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; 4.
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 Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..1697
FT /note="Serine-aspartate repeat-containing protein F"
FT /id="PRO_0000304879"
FT PROPEP 1698..1733
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000304880"
FT DOMAIN 679..797
FT /note="CNA-B 1"
FT DOMAIN 798..907
FT /note="CNA-B 2"
FT DOMAIN 908..1018
FT /note="CNA-B 3"
FT DOMAIN 1019..1129
FT /note="CNA-B 4"
FT REGION 46..678
FT /note="Ligand binding A region"
FT REGION 51..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..1129
FT /note="Type I collagen binding region"
FT REGION 862..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1694..1698
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 52..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1682
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1697
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1733 AA; 184723 MW; D8D62EA1692FD4E8 CRC64;
MKKRRQGPIN KRVDFLSNKV NKYSIRKFTV GTASILVGAT LMFGAADNEA KAAEDNQLES
ASKEEQKGSR DNENSKLNQV DLDNGSHSSE KTTNVNNATE VKKVEAPTTS DVSKPKANEA
VVTNESTKPK TTEAPTVNEE SIAETPKTST TQQDSTEKNN PSLKDNLNSS STTSKESKTD
EHSTKQAQMS TNKSNLDTND SPTQSEKTSS QANNDSTDNQ SAPSKQLDSK PSEQKVYKTK
FNDEPTQDVE HTTTKLKTPS VSTDSSVNDK QDYTRSAVAS LGVDSNETEA ITNAVRDNLD
LKAASREQIN EAIIAEALKK DFSNPDYGVD TPLALNRSQS KNSPHKSASP RMNLMSLAAE
PNSGKNVNDK VKITNPTLSL NKSNNHANNV IWPTSNEQFN LKANYELDDS IKEGDTFTIK
YGQYIRPGGL ELPAIKTQLR SKDGSIVANG VYDKTTNTTT YTFTNYVDQY QNITGSFDLI
ATPKRETAIK DNQNYPMEVT IANEVVKKDF IVDYGNKKDN TTTAAVANVD NVNNKHNEVV
YLNQNNQNPK YAKYFSTVKN GEFIPGEVKV YEVTDTNAMV DSFNPDLNSS NVKDVTSQFA
PKVSADGTRV DINFARSMAN GKKYIVTQAV RPTGTGNVYT EYWLTRDGTT NTNDFYRGTK
STTVTYLNGS STAQGDNPTY SLGDYVWLDK NKNGVQDDDE KGLAGVYVTL KDSNNRELQR
VTTDQSGHYQ FDNLQNGTYT VEFAIPDNYT PSPANNSTND AIDSDGERDG TRKVVVAKGT
INNADNMTVD TGFYLTPKYN VGDYVWEDTN KDGIQDDNEK GISGVKVTLK NKNGDTIGTT
TTDSNGKYEF TGLENGDYTI EFETPEGYTP TKQNSGSDEG KDSNGTKTTV TVKDADNKTI
DSGFYKPTYN LGDYVWEDTN KDGIQDDSEK GISGVKVTLK DKNGNAIGTT TTDASGHYQF
KGLENGSYTV EFETPSGYTP TKANSGQDIT VDSNGITTTG IINGADNLTI DSGFYKTPKY
SVGDYVWEDT NKDGIQDDNE KGISGVKVTL KDEKGNIIST TTTDENGKYQ FDNLDSGNYI
IHFEKPEGMT QTTANSGNDD EKDADGEDVR VTITDHDDFS IDNGYFDDDS DSDSDADSDS
DSDSDSDADS DSDADSDSDA DSDSDSDSDS DADSDSDSDS DSDSDSDSDA DSDSDSDSDS
DADSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDADSDS DADSDSDSDS
DSDADSDSDS DSDSDADSDS DSDSDSDSDS DSDADSDSDS DSDSDSDSDS DSDSDSDSDS
DSDADSDSDS DSDSDSDSDS DSDSDSDSDS DSDADSDADS DSDADSDSDA DSDSDSDSDS
DADSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDADS DSDSDSDSDS DSDSDADSDS
DSDSDSDADS DSDSDSDSDA DSDSDSDSDS DADSDSDSDS DSDSDSDSDA DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DADSDSDSDS DSDADSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDKNA KDKLPDTGAN EDHDSKGTLL GTLFAGLGAL LLGRRRKKDN KEK
