BBP_STAAR
ID BBP_STAAR Reviewed; 1137 AA.
AC Q6GJA6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Bone sialoprotein-binding protein;
DE Short=BSP-binding protein;
DE Flags: Precursor;
GN Name=bbp; OrderedLocusNames=SAR0567;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Specifically interacts with bone sialoprotein (BSP), a
CC glycoprotein of bone and dentin extracellular matrix. Could contribute
CC to staphylococcal osteomyelitis and arthritis (By similarity).
CC {ECO:0000250}.
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; BX571856; CAG39588.1; -; Genomic_DNA.
DR RefSeq; WP_000610336.1; NC_002952.2.
DR AlphaFoldDB; Q6GJA6; -.
DR SMR; Q6GJA6; -.
DR KEGG; sar:SAR0567; -.
DR HOGENOM; CLU_004137_1_1_9; -.
DR OMA; VTINKNY; -.
DR OrthoDB; 58491at2; -.
DR Proteomes; UP000000596; 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 3: Inferred from homology;
KW Cell wall; Peptidoglycan-anchor; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..1103
FT /note="Bone sialoprotein-binding protein"
FT /id="PRO_0000281169"
FT PROPEP 1104..1137
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000281170"
FT DOMAIN 602..714
FT /note="CNA-B 1"
FT DOMAIN 715..824
FT /note="CNA-B 2"
FT DOMAIN 825..935
FT /note="CNA-B 3"
FT REGION 53..601
FT /note="Ligand binding A region"
FT REGION 54..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1100..1104
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 73..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..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..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..1072
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1103
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1137 AA; 123326 MW; 2C7DB7BABDC8FB81 CRC64;
MINRDNKKAI TKKGMISNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAENTSTEN
AKQDEASASD NKEVVSETEN NSTQKNDLTN PIKKETNTDS HQEAKEAPTT SSTQQQQNNA
TTSTETKPQN IEKENVKPST DKTATEDTSV ILEEKKAPNN TNNDVTTKPS TSEIQTTPTT
PQESTNIENS QPQPTPSKVD NQVTDATNPK EPVNVSKEEL KNNPEKLKEL VRNDSNTDRS
TKPVATAPTS VAPKRVNAKI RFAVAQPAAV ASNNVNDLIT VTKQMITEGI KDDGVIQAHD
GEHIIYTSDF KIDNAVKAGD TMTVKYDKHT IPSDITDDFT PVDITDPSGE VIAKGTFDLN
TKTITYKFTD YVDRYENVNA KLELNSYIDK KEVPNETNLN LTFATADKET SKNVKVEYQK
PIVKDESNIQ SIFSHLDTTK HEVEQTIYVN PLKLNAKNTN VTIKSGGVAD NGDYYTGDGS
TIIDSNTEIK VYKVASGQQL PQSNKIYDYS QYEDVTNSVT INKNYGTNMA NINFGDIDSA
YIVKVVSKYT PGAEDDLAVQ QGVRMTTTNK YNYSSYAGYT NTILSTTDSG GGDGTVKPEE
KLYKIGDYVW EDVDKDGVQG TDSKEKPMAN VLVTLTYPDG TTKSVRTDAN GHYEFGGLKD
GETYTVKFET PAGYLPTKEN GTTDGEKDSN GSSVTVKING KDDMSLDTGF YKEPKYNLGD
YVWEDTNKDG IQDANEPGIK DVKVTLKDST GKVIGTTTTD ASGKYKFTDL DNGNYTVEFE
TPAGYTPTVK NTTAEDKDSN GLTTTGVIKD ADNWTLDSGF YKTPKYSLGD YVWYDSNKDG
KQDSTEKGIK DVTVTLQNEK GEVIGTTKTD ENGKYHFDNL DSGKYKVIFE KPAGLTQTGT
NTTEDDKDAD GGEVDVTITD HDDFTLDNGY FEEDTSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDAGK
HTPVKPMSAT KDHHNKAKAL PETGSENNGS NNATLFGGLF AALGSLLLFG RRKKQNK
