BBP_STAAU
ID BBP_STAAU Reviewed; 1149 AA.
AC Q14U76; Q14U55; Q9KWX6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Bone sialoprotein-binding protein;
DE Short=BSP-binding protein;
DE Flags: Precursor;
GN Name=bbp;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 326-338; 356-361;
RP 368-378; 382-390; 506-518; 549-558 AND 626-638, AND FUNCTION.
RC STRAIN=BM12987 / O24;
RX PubMed=10642520; DOI=10.1042/bj3450611;
RA Tung H.-S., Guss B., Hellman U., Persson L., Rubin K., Ryden C.;
RT "A bone sialoprotein-binding protein from Staphylococcus aureus: a member
RT of the staphylococcal sdr family.";
RL Biochem. J. 345:611-619(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=80s-2, HT20010466, HT20030336, NN1, and USA1100;
RX PubMed=16806081; DOI=10.1016/j.bbrc.2006.06.038;
RA Otsuka T., Saito K., Dohmae S., Takano T., Higuchi W., Takizawa Y.,
RA Okubo T., Iwakura N., Yamamoto T.;
RT "Key adhesin gene in community-acquired methicillin-resistant
RT Staphylococcus aureus.";
RL Biochem. Biophys. Res. Commun. 346:1234-1244(2006).
RN [3]
RP IDENTIFICATION.
RC STRAIN=BM12987 / O24;
RX PubMed=8026501; DOI=10.1111/j.1432-1033.1994.tb18940.x;
RA Yacoub A., Lindahl P., Rubin K., Wendel M., Heinegard D., Ryden C.;
RT "Purification of a bone sialoprotein-binding protein from Staphylococcus
RT aureus.";
RL Eur. J. Biochem. 222:919-925(1994).
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.
CC {ECO:0000269|PubMed:10642520}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75732.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y18653; CAB75732.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AB252195; BAE97666.1; -; Genomic_DNA.
DR EMBL; AB246404; BAE97665.1; -; Genomic_DNA.
DR EMBL; AB246403; BAE97664.1; -; Genomic_DNA.
DR EMBL; AB246402; BAE97663.1; -; Genomic_DNA.
DR EMBL; AB246401; BAE97662.1; -; Genomic_DNA.
DR RefSeq; WP_000610325.1; NZ_OGAN01000023.1.
DR PDB; 5CF3; X-ray; 2.03 A; A=272-598.
DR PDB; 5CFA; X-ray; 1.45 A; A/B=272-598.
DR PDBsum; 5CF3; -.
DR PDBsum; 5CFA; -.
DR AlphaFoldDB; Q14U76; -.
DR SMR; Q14U76; -.
DR PATRIC; fig|1280.4810.peg.1109; -.
DR PRO; PR:Q14U76; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Peptidoglycan-anchor;
KW Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..1115
FT /note="Bone sialoprotein-binding protein"
FT /id="PRO_0000288661"
FT PROPEP 1116..1149
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000288662"
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..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1112..1116
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..209
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..1084
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1115
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT VARIANT 206
FT /note="A -> T (in strain: BM12987 / O24)"
FT VARIANT 207
FT /note="I -> T (in strain: 80s-2 and BM12987 / O24)"
FT VARIANT 329
FT /note="H -> E (in strain: BM12987 / O24)"
FT VARIANT 595
FT /note="T -> S (in strain: BM12987 / O24)"
FT VARIANT 599
FT /note="E -> D (in strain: 80s-2)"
FT VARIANT 616
FT /note="D -> V (in strain: BM12987 / O24)"
FT VARIANT 698
FT /note="I -> N (in strain: 80s-2)"
FT VARIANT 876
FT /note="R -> H (in strain: BM12987 / O24)"
FT VARIANT 967
FT /note="D -> E (in strain: BM12987 / O24)"
FT VARIANT 990
FT /note="S -> SESDSDSESDSDSDSDSDSDSDS (in strain: BM12987 /
FT O24)"
FT VARIANT 1089
FT /note="D -> DSDSDSD (in strain: 80s-2)"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:5CFA"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:5CFA"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5CFA"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 375..388
FT /evidence="ECO:0007829|PDB:5CFA"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 408..417
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 427..437
FT /evidence="ECO:0007829|PDB:5CFA"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 456..468
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:5CFA"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:5CF3"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:5CFA"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 529..537
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:5CFA"
FT HELIX 553..556
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 561..568
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 572..586
FT /evidence="ECO:0007829|PDB:5CFA"
FT STRAND 589..596
FT /evidence="ECO:0007829|PDB:5CFA"
SQ SEQUENCE 1149 AA; 124570 MW; BC12B9487EF4E5C5 CRC64;
MINRDNKKAI TKKGMISNRL NKFSIRKYTV GTASILVGTT LIFGLGNQEA KAAENTSTEN
AKQDEASASD NKEVVSETEN NSTQKNDLTN PIKKETNTDS HQEAKEAPTT SSTQQQQNNA
TTSTETKPQN IEKENVKPST DKTATEDTSV ILEEKKAPNN TNNDVTTKPS TSEIQTTPTT
PQESTNIENS QPQPTPSKVD NQVTDAINPK 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 ENGKYRFDNL DSGKYKVIFE KPAGLTQTGT
NTTEDDKDAD GGEVDVTITD HDDFTLDNGY FEEDTSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS DSDSDSDSDS
DSDSDSDSDA GKHTPVKPMS ATKDHHNKAK ALPETGSENN GSNNATLFGG LFAALGSLLL
FGRRKKQNK
