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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
 
 
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