Y1996_MYCTO
ID Y1996_MYCTO Reviewed; 317 AA.
AC P9WLP0; L0T8H1; P0A5F7; Q10862;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Universal stress protein MT2052;
GN OrderedLocusNames=MT2052;
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; AAK46329.1; -; Genomic_DNA.
DR PIR; B70758; B70758.
DR RefSeq; WP_003917559.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WLP0; -.
DR SMR; P9WLP0; -.
DR EnsemblBacteria; AAK46329; AAK46329; MT2052.
DR KEGG; mtc:MT2052; -.
DR PATRIC; fig|83331.31.peg.2209; -.
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 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding.
FT CHAIN 1..317
FT /note="Universal stress protein MT2052"
FT /id="PRO_0000427445"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT BINDING 128..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT BINDING 142..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT BINDING 277..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT BINDING 291..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFD7"
SQ SEQUENCE 317 AA; 33910 MW; 16C7107048B5B33F CRC64;
MSAQQTNLGI VVGVDGSPCS HTAVEWAARD AQMRNVALRV VQVVPPVITA PEGWAFEYSR
FQEAQKREIV EHSYLVAQAH QIVEQAHKVA LEASSSGRAA QITGEVLHGQ IVPTLTNISR
QVAMVVLGYR GQGAVAGALL GSVSSSLVRH AHGPVAVIPE EPRPARPPHA PVVVGIDGSP
TSGLAAEIAF DEASRRGVDL VALHAWSDMG PLDFPRLNWA PIEWRNLEDE QEKMLARRLS
GWQDRYPDVV VHKVVVCDRP APRLLELAQT AQLVVVGSHG RGGFPGMHLG SVSRAVVNSG
QAPVIVARIP QDPAVPA