Y2175_MYCTU
ID Y2175_MYCTU Reviewed; 146 AA.
AC O53509; F2GJZ7; L0TBJ0;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=DNA-binding protein Rv2175c;
GN OrderedLocusNames=Rv2175c;
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 INTERACTION WITH PKNL, AND PHOSPHORYLATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18175374; DOI=10.1002/pmic.200700442;
RA Canova M.J., Veyron-Churlet R., Zanella-Cleon I., Cohen-Gonsaud M.,
RA Cozzone A.J., Becchi M., Kremer L., Molle V.;
RT "The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates
RT Rv2175c: mass spectrometric profiling of the activation loop
RT phosphorylation sites and their role in the recruitment of Rv2175c.";
RL Proteomics 8:521-533(2008).
RN [3]
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).
RN [4]
RP STRUCTURE BY NMR, FUNCTION, DNA-BINDING, SUBUNIT, DOMAIN, PHOSPHORYLATION
RP AT THR-9, AND MUTAGENESIS OF THR-9.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19457863; DOI=10.1074/jbc.m109.019653;
RA Cohen-Gonsaud M., Barthe P., Canova M.J., Stagier-Simon C., Kremer L.,
RA Roumestand C., Molle V.;
RT "The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-
RT binding protein regulated by phosphorylation.";
RL J. Biol. Chem. 284:19290-19300(2009).
CC -!- FUNCTION: Binds DNA at low salt concentrations.
CC {ECO:0000269|PubMed:19457863}.
CC -!- SUBUNIT: Monomer in solution. May form homodimers. Interacts with
CC phosphorylated PknL. {ECO:0000269|PubMed:18175374,
CC ECO:0000269|PubMed:19457863}.
CC -!- DOMAIN: Contains an unusual winged helix-turn-helix (wHTH) DNA-binding
CC motif missing the typical third helix. {ECO:0000269|PubMed:19457863}.
CC -!- PTM: Phosphorylated by PknL. Phosphorylation negatively regulates DNA-
CC binding activity. {ECO:0000269|PubMed:18175374,
CC ECO:0000269|PubMed:19457863}.
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DR EMBL; AL123456; CCP44952.1; -; Genomic_DNA.
DR PIR; A70936; A70936.
DR RefSeq; NP_216691.1; NC_000962.3.
DR RefSeq; WP_003900481.1; NC_000962.3.
DR PDB; 2KFS; NMR; -; A=1-146.
DR PDBsum; 2KFS; -.
DR AlphaFoldDB; O53509; -.
DR BMRB; O53509; -.
DR SMR; O53509; -.
DR STRING; 83332.Rv2175c; -.
DR iPTMnet; O53509; -.
DR PaxDb; O53509; -.
DR DNASU; 887852; -.
DR GeneID; 45426151; -.
DR GeneID; 887852; -.
DR KEGG; mtu:Rv2175c; -.
DR PATRIC; fig|83332.111.peg.2421; -.
DR TubercuList; Rv2175c; -.
DR eggNOG; ENOG5032W34; Bacteria.
DR InParanoid; O53509; -.
DR OMA; WLTLPDI; -.
DR PhylomeDB; O53509; -.
DR EvolutionaryTrace; O53509; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MTBBASE.
DR InterPro; IPR041098; Rv2175c_C.
DR Pfam; PF18367; Rv2175c_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..146
FT /note="DNA-binding protein Rv2175c"
FT /id="PRO_0000420875"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19457863"
FT MUTAGEN 9
FT /note="T->A: Lack of phosphorylation. Retains DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:19457863"
FT MUTAGEN 9
FT /note="T->D,E: Abolishes DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:19457863"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:2KFS"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2KFS"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2KFS"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:2KFS"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:2KFS"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:2KFS"
SQ SEQUENCE 146 AA; 15743 MW; 0BC42A788E105B93 CRC64;
MPGRAPGSTL ARVGSIPAGD DVLDPDEPTY DLPRVAELLG VPVSKVAQQL REGHLVAVRR
AGGVVIPQVF FTNSGQVVKS LPGLLTILHD GGYRDTEIMR WLFTPDPSLT ITRDGSRDAV
SNARPVDALH AHQAREVVRR AQAMAY
