ID FMQ_MORBO Reviewed; 157 AA. AC P07640; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 29-OCT-2014, entry version 71. DE RecName: Full=Fimbrial protein Q; DE AltName: Full=Beta pilin; DE AltName: Full=Q pilin; DE Flags: Precursor; GN Name=tfpQ; OS Moraxella bovis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND METHYLATION AT PHE-7. RC STRAIN=EPP63; RX PubMed=2861194; RA Marrs C.F., Schoolnik G., Koomey J.M., Hardy J., Rothbard J., RA Falkow S.; RT "Cloning and sequencing of a Moraxella bovis pilin gene."; RL J. Bacteriol. 163:132-139(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=EPP63; RX PubMed=2403542; RA Fulks K.A., Marrs C.F., Stevens S.P., Green M.R.; RT "Sequence analysis of the inversion region containing the pilin genes RT of Moraxella bovis."; RL J. Bacteriol. 172:310-316(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2061282; RA Rozsa F.W., Marrs C.F.; RT "Interesting sequence differences between the pilin gene inversion RT regions of Moraxella lacunata ATCC 17956 and Moraxella bovis Epp63."; RL J. Bacteriol. 173:4000-4006(1991). RN [4] RP PROTEIN SEQUENCE OF 7-157, AND DISULFIDE 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: The pili are polar flexible filaments of about 5.4 CC nanometers diameter and 2.5 micrometers average length; they CC consist of only a single polypeptide chain arranged in a helical CC configuration of five subunits per turn in the assembled pilus. CC -!- SUBCELLULAR LOCATION: Fimbrium. CC -!- MISCELLANEOUS: Moraxella bovis can express either a Q or a I CC pilin, the inversion of 2 kb of DNA determines which pilin is CC expressed. CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11435; AAA25304.1; -; Genomic_DNA. DR EMBL; M32345; AAA88223.1; -; Genomic_DNA. DR EMBL; M59712; AAA25308.1; -; Genomic_DNA. DR PIR; A24434; A24434. DR ProteinModelPortal; P07640; -. DR GO; GO:0009289; C:pilus; IEA:UniProtKB-KW. DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro. DR GO; GO:0008565; F:protein transporter activity; 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; IPR000983; Bac_GSPG_pilin. DR InterPro; IPR012902; N_methyl_site. DR InterPro; IPR001082; Pilin. DR Pfam; PF13544; N_methyl_2; 1. DR Pfam; PF00114; Pilin; 1. DR PRINTS; PR00813; BCTERIALGSPG. 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; Methylation. FT PROPEP 1 6 {ECO:0000269|PubMed:2902184}. FT /FTId=PRO_0000024148. FT CHAIN 7 157 Fimbrial protein Q. FT /FTId=PRO_0000024149. FT MOD_RES 7 7 N-methylphenylalanine. FT {ECO:0000269|PubMed:2861194}. FT DISULFID 136 155 {ECO:0000269|PubMed:2902184}. SQ SEQUENCE 157 AA; 16006 MW; A923CD8A26C693C9 CRC64; MNAQKGFTLI ELMIVIAIIG ILAAIALPAY QDYISKSQTT RVVGELAAGK TAVDAALFEG KTPKLGKAAN DTEEDIGLTT TGGTARSNLM SSVNIGGGAF ATGAGTLEAT LGNRANKDIA GAVITQSRDA EGVWTCTING SAAPGWKSKF VPTGCKE //