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Y2005_MYCTO
ID   Y2005_MYCTO             Reviewed;         295 AA.
AC   P9WLN0; L0T8C5; P64921; Q10851;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Universal stress protein MT2061;
GN   OrderedLocusNames=MT2061;
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) (at protein level) and low levels of
CC       nitric oxide (NO). {ECO:0000269|PubMed:12953092}.
CC   -!- SIMILARITY: Belongs to the universal stress protein A family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK46338.1; -; Genomic_DNA.
DR   PIR; C70759; C70759.
DR   RefSeq; WP_003410060.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WLN0; -.
DR   SMR; P9WLN0; -.
DR   EnsemblBacteria; AAK46338; AAK46338; MT2061.
DR   KEGG; mtc:MT2061; -.
DR   PATRIC; fig|83331.31.peg.2219; -.
DR   HOGENOM; CLU_049301_2_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR006015; Universal_stress_UspA.
DR   InterPro; IPR006016; UspA.
DR   Pfam; PF00582; Usp; 2.
DR   PRINTS; PR01438; UNVRSLSTRESS.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding.
FT   CHAIN           1..295
FT                   /note="Universal stress protein MT2061"
FT                   /id="PRO_0000427450"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         117..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         131..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         262..268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         276..278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
SQ   SEQUENCE   295 AA;  30985 MW;  827D60452E24BE33 CRC64;
     MSKPRKQHGV VVGVDGSLES DAAACWGATD AAMRNIPLTV VHVVNADVAT WPPMPYPETW
     GVWQEDEGRQ IVANAVKLAK EAVGADRKLS VKSELVFSTP VPTMVEISNE AEMVVLGSSG
     RGALARGLLG SVSSSLVRRA GCPVAVIHSD DAVIPDPQHA PVLVGIDGSP VSELATAVAF
     DEASRRGVEL IAVHAWSDVE VVELPGLDFS AVQQEAELSL AERLAGWQER YPDVPVSRVV
     VCDRPARKLV QKSASAQLVV VGSHGRGGLT GMLLGSVSNA VLHAARVPVI VARQS
 
 
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