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Database: UniProt
Entry: Q9X4D2_ACTNA
LinkDB: Q9X4D2_ACTNA
Original site: Q9X4D2_ACTNA 
ID   Q9X4D2_ACTNA            Unreviewed;       533 AA.
AC   Q9X4D2;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Type-1 fimbrial major subunit {ECO:0000313|EMBL:AAD28827.1};
GN   Name=fimP {ECO:0000313|EMBL:AAD28827.1};
OS   Actinomyces naeslundii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1655 {ECO:0000313|EMBL:AAD28827.1};
RN   [1] {ECO:0000313|EMBL:AAD28827.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B-1-K {ECO:0000313|EMBL:AAD28827.1};
RX   PubMed=10225854;
RA   Li T., Johansson I., Hay D.I., Stromberg N.;
RT   "Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit
RT   structurally variant fimbrial subunit proteins and bind to different
RT   peptide motifs in salivary proteins.";
RL   Infect. Immun. 67:2053-2059(1999).
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DR   EMBL; AF106035; AAD28827.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X4D2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.740; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR026466; Fim_isopep_form_D2_dom.
DR   InterPro; IPR048052; FM1-like.
DR   InterPro; IPR032364; GramPos_pilinD1_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; NF033902; iso_D2_wall_anc; 1.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   NCBIfam; TIGR04226; RrgB_K2N_iso_D2; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF16555; GramPos_pilinD1; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS51318; TAT; 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   Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..533
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039329545"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          496..533
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
SQ   SEQUENCE   533 AA;  56817 MW;  D65207B99B24528E CRC64;
     MHSLNTRRGL GLAAAMTLAA GALVAPTGAA APADPNGSTI DPDAATTLTV HKCEQTDTNG
     VKEGTGNEDP QAECKPVSDV EFTITKLNVD LTTYDGWKTL ADLKGDVVKA GALKSTTVQK
     ITTGANGLAS FTDAQTEVGA YLVSETRTPD KVIPAEDFVV TLPMTNPQDT AKWNYNVHVY
     PKNTLSGVDK QVTDKPAPGS GRDITYTITT SIPKVDYPGG ARIKRYEVVD RLDKRIKKEA
     LTPVVKIVGQ NEVTLADTTD YTLITAEGKD HNWATIQLTE EGRRKASEAR YNGNGETKLQ
     VTLTAKFDAA VNLEGDLSNT AGLIPNDSPN FTWDPNNPGT TTDIPGIPTT PVLSKYGKVV
     LTKTGTDQLA DKTKYNGAQF QVYECTKTAS GATVRDSDPS TQTVDPVTIG GEKTFTTAGQ
     GTVEINYLRA NDYVNGAKKD QLTDEDYYCL VETKAPEGYS LQADPLPFRV LAEKAEKKAA
     TEVTVTDIPK NAGFRLPLTG ANGVIFLTVA GALLVAGGAV VAYANKRRHV AKH
//
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