ID   PILIN_MYCTO             Reviewed;         103 AA.
AC   P9WI86; L0TC61; Q6MWY5; Q8VJ33;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Pilin;
DE   AltName: Full=Pili structural subunit;
DE   Flags: Precursor;
GN   Name=mtp; OrderedLocusNames=MT3413;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 90-103, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=17360408; DOI=10.1073/pnas.0602304104;
RA   Alteri C.J., Xicohtencatl-Cortes J., Hess S., Caballero-Olin G.,
RA   Giron J.A., Friedman R.L.;
RT   "Mycobacterium tuberculosis produces pili during human infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5145-5150(2007).
CC   -!- FUNCTION: Structural subunit of M.tuberculosis pili (MTP), which are
CC       thin (2- to 3-nm wide), flexible, coiled-coil, aggregative fibers. Has
CC       a strong affinity for laminin but lacks significant binding affinity
CC       for fibronectin or type IV collagen. Mediates adhesion to the
CC       extracellular matrix, an event that would facilitate direct interaction
CC       with the host epithelium during infection in the lung or other tissues.
CC       {ECO:0000269|PubMed:17360408}.
CC   -!- SUBUNIT: Forms a homomer composed of subunits assembled in a large
CC       structure. {ECO:0000269|PubMed:17360408}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:17360408}. Note=Part
CC       of the pili surface structure.
CC   -!- DEVELOPMENTAL STAGE: Is produced during infection of the human host.
CC       {ECO:0000269|PubMed:17360408}.
CC   -!- SIMILARITY: Belongs to the mycobacterial pilin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47756.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003417257.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI86; -.
DR   EnsemblBacteria; AAK47756; AAK47756; MT3413.
DR   GeneID; 45427312; -.
DR   KEGG; mtc:MT3413; -.
DR   PATRIC; fig|83331.31.peg.3672; -.
DR   HOGENOM; CLU_2260590_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell adhesion; Direct protein sequencing; Fimbrium; Signal; Virulence.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..103
FT                   /note="Pilin"
FT                   /id="PRO_0000428050"
FT   REGION          61..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   103 AA;  10768 MW;  2E02E76F1E4885D1 CRC64;
     MYRFACRTLM LAACILATGV AGLGVGAQSA AQTAPVPDYY WCPGQPFDPA WGPNWDPYTC
     HDDFHRDSDG PDHSRDYPGP ILEGPVLDDP GAAPPPPAAG GGA