ID   Y2624_MYCTO             Reviewed;         272 AA.
AC   P9WFD4; L0TD36; O06188; Q7D6V6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Universal stress protein MT2699;
GN   OrderedLocusNames=MT2699;
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: Belongs to the universal stress protein A family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47015.1; -; Genomic_DNA.
DR   PIR; G70572; G70572.
DR   RefSeq; WP_003413594.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFD4; -.
DR   SMR; P9WFD4; -.
DR   EnsemblBacteria; AAK47015; AAK47015; MT2699.
DR   KEGG; mtc:MT2699; -.
DR   PATRIC; fig|83331.31.peg.2910; -.
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; 1.
DR   PRINTS; PR01438; UNVRSLSTRESS.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
FT   CHAIN           1..272
FT                   /note="Universal stress protein MT2699"
FT                   /id="PRO_0000428558"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         109..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         123..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
SQ   SEQUENCE   272 AA;  29400 MW;  3EE3A17B3C5720DB CRC64;
     MSGRGEPTMK TIIVGIDGSH AAITAALWGV DEAISRAVPL RLVSVIKPTH PSPDDYDRDL
     AHAERSLREA QSAVEAAGKL VKIETDIPRG PAGPVLVEAS RDAEMICVGS VGIGRYASSI
     LGSTATELAE KAHCPVAVMR SKVDQPASDI NWIVVRMTDA PDNEAVLEYA AREAKLRQAP
     ILALGGRPEE LREIPDGEFE RRVQDWHHRH PDVRVYPITT HTGIARFLAD HDERVQLAVI
     GGGEAGQLAR LVGPSGHPVF RHAECSVLVV RR