ID   PILIN_MYCTA             Reviewed;         103 AA.
AC   A5U7Y7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Pilin;
DE   AltName: Full=Pili structural subunit;
DE   Flags: Precursor;
GN   Name=mtp; OrderedLocusNames=MRA_3354;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
RN   [2]
RP   FUNCTION IN PILI FORMATION, SUBCELLULAR LOCATION, AND SUBUNIT.
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, flexible, coiled-coil, aggregative fibers. Mediates adhesion to
CC       the extracellular matrix (Probable). {ECO:0000305|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   -!- SIMILARITY: Belongs to the mycobacterial pilin family. {ECO:0000305}.
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DR   EMBL; CP000611; ABQ75137.1; -; Genomic_DNA.
DR   RefSeq; WP_003417257.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U7Y7; -.
DR   STRING; 419947.MRA_3354; -.
DR   EnsemblBacteria; ABQ75137; ABQ75137; MRA_3354.
DR   GeneID; 45427312; -.
DR   KEGG; mra:MRA_3354; -.
DR   eggNOG; ENOG5031U6Y; Bacteria.
DR   HOGENOM; CLU_2260590_0_0_11; -.
DR   OMA; WEFGECH; -.
DR   OrthoDB; 2092705at2; -.
DR   Proteomes; UP000001988; 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; Fimbrium; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..103
FT                   /note="Pilin"
FT                   /id="PRO_0000314592"
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