Y1996_MYCTU
ID Y1996_MYCTU Reviewed; 317 AA.
AC P9WLP1; 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 37.
DE RecName: Full=Universal stress protein Rv1996;
DE Short=USP Rv1996;
GN OrderedLocusNames=Rv1996; ORFNames=MTCY39.23c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [3]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA Shiloh M.U., Manzanillo P., Cox J.S.;
RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT macrophage infection.";
RL Cell Host Microbe 3:323-330(2008).
RN [4]
RP INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA Agarwal A., Steyn A.J.;
RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT tuberculosis dormancy regulon.";
RL J. Biol. Chem. 283:18032-18039(2008).
RN [5]
RP PUPYLATION AT LYS-88, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20541977; DOI=10.1016/j.tube.2010.03.013;
RA Hingley-Wilson S.M., Lougheed K.E., Ferguson K., Leiva S., Williams H.D.;
RT "Individual Mycobacterium tuberculosis universal stress protein homologues
RT are dispensable in vitro.";
RL Tuberculosis 90:236-244(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and
CC carbon monoxide (CO). It is hoped that this regulon will give insight
CC into the latent, or dormant phase of infection.
CC {ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:18400743,
CC ECO:0000269|PubMed:18474359}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal or hypoxic and
CC normoxic stationary phase growth, nor in mouse- or human-derived
CC macrophage cell lines. {ECO:0000269|PubMed:20541977}.
CC -!- SIMILARITY: Belongs to the universal stress protein A family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44768.1; -; Genomic_DNA.
DR PIR; B70758; B70758.
DR RefSeq; NP_216512.1; NC_000962.3.
DR RefSeq; WP_003899121.1; NZ_NVQJ01000043.1.
DR AlphaFoldDB; P9WLP1; -.
DR SMR; P9WLP1; -.
DR STRING; 83332.Rv1996; -.
DR PaxDb; P9WLP1; -.
DR DNASU; 888863; -.
DR GeneID; 888863; -.
DR KEGG; mtu:Rv1996; -.
DR TubercuList; Rv1996; -.
DR eggNOG; COG0589; Bacteria.
DR OMA; HIPAFYY; -.
DR PhylomeDB; P9WLP1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; Isopeptide bond; Nucleotide-binding; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..317
FT /note="Universal stress protein Rv1996"
FT /id="PRO_0000103924"
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"
FT CROSSLNK 88
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
SQ SEQUENCE 317 AA; 33880 MW; 0DCDB0CA530F138E CRC64;
MSAQQTNLGI VVGVDGSPCS HTAVEWAARD AQMRNVALRV VQVVPPVITA PEGWAFEYSR
FQEAQKREIV EHSYLVAQAH QIVEQAHKVA LEASSSGRAA QITGEVLHGQ IVPTLANISR
QVAMVVLGYR GQGAVAGALL GSVSSSLVRH AHGPVAVIPE EPRPARPPHA PVVVGIDGSP
TSGLAAEIAF DEASRRGVDL VALHAWSDMG PLDFPRLNWA PIEWRNLEDE QEKMLARRLS
GWQDRYPDVV VHKVVVCDRP APRLLELAQT AQLVVVGSHG RGGFPGMHLG SVSRAVVNSG
QAPVIVARIP QDPAVPA
