ID   FM2_ACTNA               Reviewed;         534 AA.
AC   P12616;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Fimbrial subunit type 2;
DE   Flags: Precursor;
OS   Actinomyces naeslundii.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinomyces.
OX   NCBI_TaxID=1655;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WVU45;
RX   PubMed=2900829; DOI=10.1128/jb.170.9.3803-3809.1988;
RA   Yeung M.K., Cisar J.O.;
RT   "Cloning and nucleotide sequence of a gene for Actinomyces naeslundii WVU45
RT   type 2 fimbriae.";
RL   J. Bacteriol. 170:3803-3809(1988).
CC   -!- FUNCTION: Major fimbrial subunit of A.naeslundii.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}. Fimbrium {ECO:0000305}.
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DR   EMBL; M21976; AAA21931.1; -; Genomic_DNA.
DR   PIR; A32347; A32347.
DR   AlphaFoldDB; P12616; -.
DR   SMR; P12616; -.
DR   PRIDE; P12616; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR026466; Fim_isopep_form_D2_dom.
DR   InterPro; IPR032364; GramPos_pilinD1_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF16555; GramPos_pilinD1; 1.
DR   TIGRFAMs; TIGR04226; RrgB_K2N_iso_D2; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall; Fimbrium; Peptidoglycan-anchor; Secreted; Signal.
FT   SIGNAL          1..32
FT   CHAIN           33..495
FT                   /note="Fimbrial subunit type 2"
FT                   /id="PRO_0000005603"
FT   PROPEP          496..534
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005604"
FT   REGION          56..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           492..496
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        362..376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         495
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   534 AA;  56574 MW;  6C56C3AB493D5751 CRC64;
     MKYNTSTLGR RAAAAAGVLT LAVLGLAPMA QAENANHGDI NTEALGSLTI HKHLNGDGNP
     IGAPDGTASN DDGKGAPVSG VQFTAYEING IDLKTSEGWA KVNALTNTGA IPDNACANPG
     QPTLPNYTFR SSRVSGDTDR DGEAKIESLP VKAYLVCETK TPGNIVQKAK PFVVTIPHPN
     TAAKADGTWL YDVHVYPKNE KIEVAKTIED QRNNGYIVGS KVRFPVSSTL PKLDDNSYYK
     YYQFKDTLDN RLKQVTATDV TLGGTRLDEG TDYTLGTDGQ TVTVTFNQNG LSKLKGNPGQ
     KLQAVFEGVV SEVGDGSINN TAQLISDTTY AEQPPAPETP PANPDNPPTT EQVTSKWGDL
     TIKKVDGNDR SGDKDGLKGA EFQIYKAKDA YADTCSPEAD GQPLTINGES TFTTGEGGTI
     NFKALFVSDS VQDTGRDNRV DAPHRCYVLV ETKAPAGYVL PADASRAITV EPGAGVTQQV
     VIDNVKQSVP GLPLTGANGM LILTASGAAL LMIAVGSVLV ARYRERKRNR DLAA