ID   D2Q781_BIFDB            Unreviewed;      1256 AA.
AC   D2Q781;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=Fimbriae protein with LPXTG motif and von Willebrand factor typeA domain {ECO:0000313|EMBL:ADB08827.1};
GN   OrderedLocusNames=BDP_0143 {ECO:0000313|EMBL:ADB08827.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB08827.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB08827.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
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DR   EMBL; CP001750; ADB08827.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2Q781; -.
DR   STRING; 401473.BDP_0143; -.
DR   KEGG; bde:BDP_0143; -.
DR   eggNOG; COG1361; Bacteria.
DR   eggNOG; COG2304; Bacteria.
DR   HOGENOM; CLU_278345_0_0_11; -.
DR   Proteomes; UP000008693; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd00198; vWFA; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.3050; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR047589; DUF11_rpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR022464; Strep_pil_isopept_link.
DR   InterPro; IPR038174; Strep_pil_link_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   NCBIfam; TIGR01451; B_ant_repeat; 1.
DR   Pfam; PF12892; FctA; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   4: Predicted;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008693};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1228..1249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          592..823
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1217..1256
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          47..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1256 AA;  132715 MW;  9E5D779A14F6844C CRC64;
     MKRACDEWQA VRKGGLAKRV ITALVAVAML GGLGYATAST AVAQDDTTQQ QAQQTEQSAK
     TTSESQDEKT SDSEATSKKA ATDETSADGS AEDTNTTDAD AGVEAQNGAD ETAVQAANEP
     AATSVADGGS PESGSLLLDE SFKNSTFGDA NWTTADSACL TAATSGSLKC ENTQDSSDIQ
     GENGKGYLQL TDNSENQKAA VLYNQPVISK SGLHVTFDYY MYQTSGAGKY TTPADGISFF
     LTDGAATLSK AGTSGAALGY ATSDDDGIGD SSKRGEGVAQ GVLGIGFDRF GNFSTQHAAG
     TTARVTGGDD CTQSGTNAGN SVTVRGAGKI DVDGKWNNGY CIVASENVAA GLDSGKATKS
     ENDTNGESVD ITIAPVIDDS ATTQHLTVKI AGETVLEKDI DRLPDSVKFG FSASTGADHQ
     VQLIRGLKVY SVNKLSQLDL VKSMNKDTYP DADSHTFNVG DEVPYTFVVR NSGTTTLNNV
     AVNDPNITNV SCGTDTLAAN QQTTCSGTLT LTEDMVDSEG HFTNTATASG TDDEGNAVNS
     PQASVTIKAI KPLGAPEKHK RIKKNSDNTY TVNVDVTGAA NSSTITTTQS VDFTLVLDVS
     SSMSDEMDSD QGSIKKMTAL KSAVNNFLGE AAEINEQSGS ELIRVGLVKF AGKESSKVGN
     ETYTEGRFVY NYSQIVSPLT ADMSDLKNKV SALRHNGATR ADLGFKHAST VMSGARTDAK
     RVVIFFTDGT PTKVSDFDKD VANSAVTYAK SLKDSGATVY SIGVFDGANP SSIEENQKNQ
     FMNAVSSNYP HATAYDKLGT GSNAGYYKVV SNVSDLKSIF EKIQTNETTD GFTNVSIEDT
     LSKYVELSGK NYTVTAKDAN GNEVTLKENS DYTLTYDESA KKFTVVFQNM LQDGVTYTLS
     YNVKPTQEAY DEYAANGYGG TVGDADTDLD GSTTSSGQLG FHSNESACLA YTANGKRHVC
     SDNPYLHPVI QVVSSTLHIE KQWSGDGEKP ASINVTIKQG NSDYKTVTLT PDDNGNWSTD
     VIIPAGESKT YTVTENDPGN QWNVSYQHKV GDGNLADGNA VTVPQSATSQ TATVIVTNKQ
     ALVTLPADSI TVNKKVVGTN TGHDFNFTMI ATGDNAGKVT WPRTDQSKSK VTISQVSQTQ
     VKSATFGDEL TFPAANATYT FQVTEDKPTD TTGWKYDDSE QTVTVTVSYD ETQKKWTAVA
     SPAEVTFTNR YIAVASLPLT GGTTDRQWLM IGGGIAGMAM LMIGAAGIWR GRKRLV
//