ID   Y2623_MYCTO             Reviewed;         297 AA.
AC   P9WFD6; L0TAF1; O06189; Q7D6V7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Universal stress protein MT2698;
GN   OrderedLocusNames=MT2698;
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   -!- FUNCTION: May play a role in the establishment of a persistent
CC       infection (latency) in the host. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK47014.1; -; Genomic_DNA.
DR   PIR; F70572; F70572.
DR   RefSeq; WP_003413592.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFD6; -.
DR   SMR; P9WFD6; -.
DR   EnsemblBacteria; AAK47014; AAK47014; MT2698.
DR   KEGG; mtc:MT2698; -.
DR   PATRIC; fig|83331.31.peg.2909; -.
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; Virulence.
FT   CHAIN           1..297
FT                   /note="Universal stress protein MT2698"
FT                   /id="PRO_0000428557"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P9WFD7"
FT   BINDING         43
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         127
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   297 AA;  31652 MW;  A590F7058D1E8695 CRC64;
     MSSGNSSLGI IVGIDDSPAA QVAVRWAARD AELRKIPLTL VHAVSPEVAT WLEVPLPPGV
     LRWQQDHGRH LIDDALKVVE QASLRAGPPT VHSEIVPAAA VPTLVDMSKD AVLMVVGCLG
     SGRWPGRLLG SVSSGLLRHA HCPVVIIHDE DSVMPHPQQA PVLVGVDGSS ASELATAIAF
     DEASRRNVDL VALHAWSDVD VSEWPGIDWP ATQSMAEQVL AERLAGWQER YPNVAITRVV
     VRDQPARQLV QRSEEAQLVV VGSRGRGGYA GMLVGSVGET VAQLARTPVI VARESLT