SDRF_STAES
ID SDRF_STAES Reviewed; 1633 AA.
AC Q8CMP4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Serine-aspartate repeat-containing protein F;
DE Flags: Precursor;
GN Name=sdrF; OrderedLocusNames=SE_2395;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Binds to type I collagen via alpha-2(I) or alpha-1(I) chains.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; AE015929; AAO06038.1; -; Genomic_DNA.
DR RefSeq; NP_765950.1; NC_004461.1.
DR RefSeq; WP_011082831.1; NC_004461.1.
DR AlphaFoldDB; Q8CMP4; -.
DR SMR; Q8CMP4; -.
DR STRING; 176280.SE_2395; -.
DR EnsemblBacteria; AAO06038; AAO06038; SE_2395.
DR KEGG; sep:SE_2395; -.
DR PATRIC; fig|176280.10.peg.2335; -.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR eggNOG; COG4932; Bacteria.
DR HOGENOM; CLU_004137_0_1_9; -.
DR OMA; GAQIKIF; -.
DR Proteomes; UP000001411; 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; -; 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 3: Inferred from homology;
KW Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..1597
FT /note="Serine-aspartate repeat-containing protein F"
FT /id="PRO_0000304881"
FT PROPEP 1598..1633
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000304882"
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 679..1129
FT /note="Type I collagen binding region"
FT /evidence="ECO:0000250"
FT REGION 862..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1594..1598
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 866..889
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..1582
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1597
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1633 AA; 174771 MW; DAA8537B8CD288BD CRC64;
MKKRRQGPIN KRVDFLSNKV NKYSIRKFTV GTASILVGAT LMFGAADNEA KAAEDNQLES
ASKEEQKGSR DNESSKLNQV DLDNGSHSSE KTTNVNNATE VKKVEAPTTS DVSKPKANEA
VVTNESTKPK TTEAPTVNEE SIAETPKTST TQQDSTEKNN PSLKDNLNSS STTSKESKTD
EHSTKQAQMS TNKSNLDTND SPTQSEKTSS QANNDSTDNQ SAPSKQLDSK PSEQKVYKTK
FNDEPTQDVE HTTTKLKTPS ISTDSSVNDK QDYTRSAVAS LGVDSNETEA ITNAVRDNLD
LKAASREQIN EAIIAEALKK DFSNPDYGVD TPLALNTSQS KNSPHKSASP RMNLMSLAAE
PNSGKNVNDK VKITNPTLSL NKSNNHANNV IWPTSNEQFN LKANYELDDS IKEGDTFTIK
YGQYIRPGGL ELPAIKTQLR SKDGSIVANG VYDKTTNTTT YTFTNYVDQY QNITGSFDLI
ATPKRETAIK DNQNYPMEVT IANEVVKKDF IVDYGNKKDN TTTAAVANVD NVNNKHNEVV
YLNQNNQNPK YAKYFSTVKN GKFIPGEVKV YEVTDTNAMV DSFNPDLNSS NVKDVTSQFT
PKVSADGTRV DINFARSMAN GKKYIVTQAV RPTGTGNVYT EYWLTRDGTT NTNDFYRGTK
STTVTYLNGS STAQGDNPTY SLGDYVWLDK NKNGVQDDDE KGLAGVYVTL KDSNNRELQR
VTTDQSGHYQ FDNLQNGTYT VEFAIPDNYT PSPANNSTND AIDSDGERDG TRKVVVAKGT
INNADNMTVD TGFYLTPKYN VGDYVWEDTN KDGIQDDNEK GISNVKVTLK NKNGDTIGTT
TTDSNGKYEF TGLENGDYTI EFETPEGYTP TKQNSGSDEG KDSNGTKTTV TVKDADNKTI
DSGFYKPIYN LGDYVWEDTN KDGIQDDSEK GISGVKVTLK DKNGNAIGTT TTDASGHYQF
KGLENGSYTV EFETPSGYTP TKANSGQDIT VDSNGITTTG IINGADNLTI DSGFYKTPKY
SVGDYVWEDT NKDGIQDDNE KGISGVKVTL KDEKGNIIST TTTDENGKYQ FDNLDSGNYI
IHFEKPEGMT QTTANSGNDD EKDADGEDVR VTITDHDDFS IDNGYFDDDS DSDSDADSDS
DSDSDSDADS DSDADSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDADSDS DADSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDADSDSDA DSDSDADSDS DADSDSDSDS DSDADSDSDS
DSDSDADSDS DSDSDSDADS DSDSDSDSDA DSDSDSDSDS DADSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDADSDS DSDSDSDADS DSDADSDSDS DSDSDSDSDS
DADSDSDSDS DSDSDSDSDA DSDSDSDSDS DAESDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDADS DSDSDSDSDS DSDSDSDSDS DSDSDSDADS DSYSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDKNA KDKLPDTGAN EDHDSKGTLL GTLFAGLGAL
LLGRRRKKDN KEK
