PILIN_MYCTU
ID PILIN_MYCTU Reviewed; 103 AA.
AC P9WI87; 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 31.
DE RecName: Full=Pilin;
DE AltName: Full=Pili structural subunit;
DE Flags: Precursor;
GN Name=mtp; OrderedLocusNames=Rv3312.1; ORFNames=Rv3312A;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 90-103, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [3]
RP INDUCTION BY PHOP.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16573683; DOI=10.1111/j.1365-2958.2006.05102.x;
RA Walters S.B., Dubnau E., Kolesnikova I., Laval F., Daffe M., Smith I.;
RT "The Mycobacterium tuberculosis PhoPR two-component system regulates genes
RT essential for virulence and complex lipid biosynthesis.";
RL Mol. Microbiol. 60:312-330(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- INDUCTION: Positively regulated by PhoP. {ECO:0000269|PubMed:16573683}.
CC -!- SIMILARITY: Belongs to the mycobacterial pilin family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46132.1; -; Genomic_DNA.
DR RefSeq; WP_003417257.1; NZ_NVQJ01000003.1.
DR RefSeq; YP_177957.1; NC_000962.3.
DR AlphaFoldDB; P9WI87; -.
DR STRING; 83332.Rv3312A; -.
DR PaxDb; P9WI87; -.
DR GeneID; 3205113; -.
DR GeneID; 45427312; -.
DR KEGG; mtu:Rv3312A; -.
DR TubercuList; Rv3312A; -.
DR eggNOG; ENOG5031U6Y; Bacteria.
DR OMA; WEFGECH; -.
DR PHI-base; PHI:7452; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009289; C:pilus; IDA:MTBBASE.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0009297; P:pilus assembly; IMP:MTBBASE.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Fimbrium; Reference proteome;
KW Signal; Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..103
FT /note="Pilin"
FT /id="PRO_0000314591"
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