ID   FMM_MORNO               Reviewed;         154 AA.
AC   P09829;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Fimbrial protein;
DE   AltName: Full=Pilin;
DE   Flags: Precursor;
GN   Name=tfpA;
OS   Moraxella nonliquefaciens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCTC 7784;
RX   PubMed=1770363; DOI=10.1099/00221287-137-10-2483;
RA   Tonjum T., Marrs C.F., Rozsa F.W., Bovre K.;
RT   "The type 4 pilin of Moraxella nonliquefaciens exhibits unique similarities
RT   with the pilins of Neisseria gonorrhoeae and Dichelobacter (Bacteroides)
RT   nodosus.";
RL   J. Gen. Microbiol. 137:2483-2490(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 7-55, AND METHYLATION AT PHE-7.
RX   PubMed=838045; DOI=10.1016/0014-5793(77)80008-2;
RA   Froholm L.O., Sletten K.;
RT   "Purification and N-terminal sequence of a fimbrial protein from Moraxella
RT   nonliquefaciens.";
RL   FEBS Lett. 73:29-32(1977).
CC   -!- SUBUNIT: The pili are polar flexible filaments of about 5.4 nanometers
CC       diameter and 2.5 micrometers average length; they consist of only a
CC       single polypeptide chain arranged in a helical configuration of five
CC       subunits per turn in the assembled pilus.
CC   -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
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DR   EMBL; M59707; AAA25310.1; -; Genomic_DNA.
DR   PIR; A44809; A44809.
DR   AlphaFoldDB; P09829; -.
DR   SMR; P09829; -.
DR   iPTMnet; P09829; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 3.30.700.10; Glycoprotein, Type 4 Pilin; 1.
DR   InterPro; IPR012902; N_methyl_site.
DR   InterPro; IPR001082; Pilin.
DR   InterPro; IPR045584; Pilin-like.
DR   NCBIfam; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PANTHER; PTHR30093; GENERAL SECRETION PATHWAY PROTEIN G; 1.
DR   PANTHER; PTHR30093:SF34; TYPE IV MAJOR PILIN PROTEIN PILA; 1.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF00114; Pilin; 1.
DR   SUPFAM; SSF54523; Pili subunits; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Fimbrium; Membrane; Methylation; Transmembrane;
KW   Transmembrane helix.
FT   PROPEP          1..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT                   ECO:0000269|PubMed:838045"
FT                   /id="PRO_0000024152"
FT   CHAIN           7..154
FT                   /note="Fimbrial protein"
FT                   /id="PRO_0000024153"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT                   ECO:0000269|PubMed:838045"
SQ   SEQUENCE   154 AA;  16467 MW;  80BE4B0815563E0F CRC64;
     MNAQKGFTLI ELMIVIAIIG ILAAIALPAY QDYIARAQVS EAFTLADGLK TSISTNRQNG
     RCFADGKDTA ADGVDIITGK YGKATILEEN PNTADGLICG IYYEFNTTGV SDKLIGKTIA
     LKADEKAGKL VLETVNSKTT NVENKYLPSA FKKP
//