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