FMI_MORBO
ID FMI_MORBO Reviewed; 159 AA.
AC P20657;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Type IV major alpha-pilin;
DE AltName: Full=Alpha-pilin;
DE AltName: Full=Fimbrial protein I;
DE AltName: Full=I pilin;
DE Flags: Precursor;
GN Name=tfpI;
OS Moraxella bovis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EPP63;
RX PubMed=2403542; DOI=10.1128/jb.172.1.310-316.1990;
RA Fulks K.A., Marrs C.F., Stevens S.P., Green M.R.;
RT "Sequence analysis of the inversion region containing the pilin genes of
RT Moraxella bovis.";
RL J. Bacteriol. 172:310-316(1990).
RN [2]
RP PROTEIN SEQUENCE OF 7-159, METHYLATION AT PHE-7, FUNCTION, AND DISULFIDE
RP BOND.
RX PubMed=2902184; DOI=10.1084/jem.168.3.983;
RA Ruehl W.W., Marrs C.F., Fernandez R., Falkow S., Schoolnik G.K.;
RT "Purification, characterization, and pathogenicity of Moraxella bovis
RT pili.";
RL J. Exp. Med. 168:983-1002(1988).
CC -!- SUBUNIT: Major component of the type IV pilus (T4P) that plays a role
CC in surface and attachment to the host epithelial tissues.
CC {ECO:0000269|PubMed:2902184}.
CC -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Moraxella bovis can express either a Q or a I pilin, the
CC inversion of 2 kb of DNA determines which pilin is expressed.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR EMBL; M32345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JL0071; JL0071.
DR AlphaFoldDB; P20657; -.
DR SMR; P20657; -.
DR STRING; 476.B0182_10750; -.
DR iPTMnet; P20657; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR001082; Pilin.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF00114; Pilin; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Fimbrium; Membrane; Methylation;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..6
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:2902184"
FT /id="PRO_0000024150"
FT CHAIN 7..159
FT /note="Type IV major alpha-pilin"
FT /id="PRO_0000024151"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 64..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:2902184"
FT DISULFID 137..156
FT /evidence="ECO:0000269|PubMed:2902184"
FT CONFLICT 159
FT /note="K -> KSK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 16723 MW; 9130E2289C7F679E CRC64;
MNAQKGFTLI ELMIVIAIIG ILAAIALPAY QDYISKSQTT RVSGELAAGK TAVDAALFEG
KTPVLSEESS TSKENIGLTS SETSTKPRSN LMASVELTGF ADNGAGTISA TLGNKANKDI
AKTVITQERT TDGVWTCKID GSQAAKYKEK FNPTGCVKK
