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Database: UniProt
Entry: Y485_MYCTU
LinkDB: Y485_MYCTU
Original site: Y485_MYCTU 
ID   Y485_MYCTU              Reviewed;         438 AA.
AC   P9WKV1; L0T5I1; P64705; Q11151;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Transcriptional regulator Rv0485 {ECO:0000305};
GN   OrderedLocusNames=Rv0485; ORFNames=MTCY20G9.11;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=H37Rv;
RX   PubMed=19651861; DOI=10.1128/iai.01495-08;
RA   Goldstone R.M., Goonesekera S.D., Bloom B.R., Sampson S.L.;
RT   "The transcriptional regulator Rv0485 modulates the expression of a pe and
RT   ppe gene pair and is required for Mycobacterium tuberculosis virulence.";
RL   Infect. Immun. 77:4654-4667(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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: Positively regulates the expression of PE13 and PPE18. Can
CC       also regulate expression of some other genes. Plays a role in
CC       modulation of innate immune responses. {ECO:0000269|PubMed:19651861}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene reduces the expression of
CC       PE13 and PPE18. It allows mice to survive for significant longer, with
CC       substantially reduced lung pathology. {ECO:0000269|PubMed:19651861}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43219.1; -; Genomic_DNA.
DR   PIR; H70743; H70743.
DR   RefSeq; NP_214999.1; NC_000962.3.
DR   RefSeq; WP_003402361.1; NZ_NVQJ01000002.1.
DR   AlphaFoldDB; P9WKV1; -.
DR   SMR; P9WKV1; -.
DR   STRING; 83332.Rv0485; -.
DR   PaxDb; 83332-Rv0485; -.
DR   DNASU; 887170; -.
DR   GeneID; 887170; -.
DR   KEGG; mtu:Rv0485; -.
DR   TubercuList; Rv0485; -.
DR   eggNOG; COG1940; Bacteria.
DR   InParanoid; P9WKV1; -.
DR   OrthoDB; 3605644at2; -.
DR   PhylomeDB; P9WKV1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:MTBBASE.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR18964:SF177; N-ACETYLMANNOSAMINE KINASE; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..438
FT                   /note="Transcriptional regulator Rv0485"
FT                   /id="PRO_0000103687"
FT   DNA_BIND        52..73
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000305|PubMed:19651861"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   438 AA;  46099 MW;  D75B8F6777DE1E6F CRC64;
     MYSTNRTSQS LSRKPGRKHQ LRSHRYVMPP SLHLSDSAAA SVFRAVRLRG PVGRDVIAGS
     TSLSIATVNR QVIALLEAGL LRERADLAVS GAIGRPRVPV EVNHEPFVTL GIHIGARTTS
     IVATDLFGRT LDTVETPTPR NAAGAALTSL ADSADRYLQR WRRRRALWVG VTLGGAVDSA
     TGHVDHPRLG WRQAPVGPVL ADALGLPVSV ASHVDAMAGA ELMLGMRRFA PSSSTSLYVY
     ARETVGYALM IGGRVHCPAS GPGTIAPLPV HSEMLGGTGQ LESTVSDEAV LAAARRLRII
     PGIASRTRTG GSATAITDLL RVARAGNQQA KELLAERARV LGGAVALLRD LLNPDEVVVG
     GQAFTEYPEA MEQVEAAFTA GSVLAPRDIR VTVFGNRVQE AGAGIVSLSG LYADPLGALR
     RSGALDARLQ DTAPEALA
//
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