Y2030_MYCTO
ID Y2030_MYCTO Reviewed; 681 AA.
AC P9WLM0; L0T8K6; O53475; Q7D7L3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Uncharacterized protein MT2089;
GN OrderedLocusNames=MT2089;
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 INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC {ECO:0000269|PubMed:12953092}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46368.1; -; Genomic_DNA.
DR PIR; E70942; E70942.
DR RefSeq; WP_003410178.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WLM0; -.
DR SMR; P9WLM0; -.
DR EnsemblBacteria; AAK46368; AAK46368; MT2089.
DR KEGG; mtc:MT2089; -.
DR PATRIC; fig|83331.31.peg.2253; -.
DR HOGENOM; CLU_015623_1_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR CDD; cd14728; Ere-like; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR007815; Emycin_Estase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF05139; Erythro_esteras; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
PE 2: Evidence at transcript level;
KW Transferase.
FT CHAIN 1..681
FT /note="Uncharacterized protein MT2089"
FT /id="PRO_0000427455"
SQ SEQUENCE 681 AA; 74930 MW; 82DAC6ACC5550947 CRC64;
MLMTAAADVT RRSPRRVFRD RREAGRVLAE LLAAYRDQPD VIVLGLARGG LPVAWEVAAA
LHAPLDAFVV RKLGAPGHDE FAVGALASGG RVVVNDDVVR GLRITPQQLR DIAEREGREL
LRRESAYRGE RPPTDITGKT VIVVDDGLAT GASMFAAVQA LRDAQPAQIV IAVPAAPEST
CREFAGLVDD VVCATMPTPF LAVGESFWDF RQVTDEEVRR LLATPTAGPS LRRPAASTAA
DVLRRVAIDA PGGVPTHEVL AELVGDARIV LIGESSHGTH EFYQARAAMT QWLIEEKGFG
AVAAEADWPD AYRVNRYVRG LGEDTNADEA LSGFERFPAW MWRNTVVRDF VEWLRTRNQR
YESGALRQAG FYGLDLYSLH RSIQEVISYL DKVDPRAAAR ARARYACFDH ACADDGQAYG
FAAAFGAGPS CEREAVEQLV DVQRNALAYA RQDGLLAEDE LFYAQQNAQT VRDAEVYYRA
MFSGRVTSWN LRDQHMAQTL GSLLTHLDRH LDAPPARIVV WAHNSHVGDA RATEVWADGQ
LTLGQIVRER YGDESRSIGF STYTGTVTAA SEWGGIAQRK AVRPALHGSV EELFHQTADS
FLVSARLSRD AEAPLDVVRL GRAIGVVYLP ATERQSHYLH VRPADQFDAM IHIDQTRALE
PLEVTSRWIA GENPETYPTG L