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FIMA_DICNV
ID   FIMA_DICNV              Reviewed;         162 AA.
AC   A5EWR9;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Type IV major fimbrial protein FimA;
DE   Flags: Precursor;
GN   Name=fimA; OrderedLocusNames=DNO_0110;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11443078; DOI=10.1128/jb.183.15.4451-4458.2001;
RA   Kennan R.M., Dhungyel O.P., Whittington R.J., Egerton J.R., Rood J.I.;
RT   "The type IV fimbrial subunit gene (fimA) of Dichelobacter nodosus is
RT   essential for virulence, protease secretion, and natural competence.";
RL   J. Bacteriol. 183:4451-4458(2001).
RN   [3]
RP   INDUCTION BY RPON AND PILR.
RC   STRAIN=VCS1703A;
RX   PubMed=16788189; DOI=10.1128/jb.00255-06;
RA   Parker D., Kennan R.M., Myers G.S., Paulsen I.T., Songer J.G., Rood J.I.;
RT   "Regulation of type IV fimbrial biogenesis in Dichelobacter nodosus.";
RL   J. Bacteriol. 188:4801-4811(2006).
RN   [4]
RP   FUNCTION.
RC   STRAIN=VCS1703A;
RX   PubMed=17513472; DOI=10.1128/jb.00138-07;
RA   Han X., Kennan R.M., Parker D., Davies J.K., Rood J.I.;
RT   "Type IV fimbrial biogenesis is required for protease secretion and natural
RT   transformation in Dichelobacter nodosus.";
RL   J. Bacteriol. 189:5022-5033(2007).
RN   [5]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=VCS1703A;
RX   PubMed=18310333; DOI=10.1128/jb.01807-07;
RA   Han X., Kennan R.M., Davies J.K., Reddacliff L.A., Dhungyel O.P.,
RA   Whittington R.J., Turnbull L., Whitchurch C.B., Rood J.I.;
RT   "Twitching motility is essential for virulence in Dichelobacter nodosus.";
RL   J. Bacteriol. 190:3323-3335(2008).
CC   -!- FUNCTION: Major component of the type IV fimbriae that plays an
CC       essential role in twitching motility, natural transformation, and
CC       protease secretion. {ECO:0000269|PubMed:11443078,
CC       ECO:0000269|PubMed:17513472, ECO:0000269|PubMed:18310333}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:18310333}. Membrane
CC       {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: By PilR (PilR/S system) and RNA polymerase sigma-54
CC       factor/RpoN. {ECO:0000269|PubMed:16788189}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutants do not colonize the ovine hoof.
CC       Mutants show also altered secretion of extracellular proteases and
CC       twitching motility. {ECO:0000269|PubMed:11443078}.
CC   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR   EMBL; CP000513; ABQ13217.1; -; Genomic_DNA.
DR   RefSeq; WP_011927861.1; NC_009446.1.
DR   AlphaFoldDB; A5EWR9; -.
DR   SMR; A5EWR9; -.
DR   STRING; 246195.DNO_0110; -.
DR   EnsemblBacteria; ABQ13217; ABQ13217; DNO_0110.
DR   KEGG; dno:DNO_0110; -.
DR   eggNOG; COG4969; Bacteria.
DR   HOGENOM; CLU_091705_4_2_6; -.
DR   OrthoDB; 1970253at2; -.
DR   Proteomes; UP000000248; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR001082; Pilin.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR002416; T2SS_protein-GspH.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF00114; Pilin; 1.
DR   PRINTS; PR00885; BCTERIALGSPH.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Fimbrium; Membrane; Methylation; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   PROPEP          1..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000450771"
FT   CHAIN           8..162
FT                   /note="Type IV major fimbrial protein FimA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000450772"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         8
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   DISULFID        63..106
FT                   /evidence="ECO:0000250|UniProtKB:P02975"
SQ   SEQUENCE   162 AA;  17002 MW;  9D833357883D3EFD CRC64;
     MKSLQKGFTL IELMIVVAII GILAAFAIPA YNDYIARTQV SEGVSLADGL KIRIADNLQD
     GKCTSEGDPA SGEVGNTDMG KYALATIEGT PDANLAGLTP KDPNGCKVKI EYGKGTAGDN
     ISPLIKGQML VLNQLVNGSY DKDSSSTVKP KFLPKALKEA TP
 
 
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