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Universal stress protein Rv1996 (USP Rv1996)

 Y1996_MYCTU             Reviewed;         317 AA.
P9WLP1; L0T8H1; P0A5F7; Q10862;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
20-JUN-2018, entry version 21.
RecName: Full=Universal stress protein Rv1996;
Short=USP Rv1996;
OrderedLocusNames=Rv1996; ORFNames=MTCY39.23c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12953092; DOI=10.1084/jem.20030205;
Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I.,
Dolganov G.M., Sherman D.R., Schoolnik G.K.;
"Inhibition of respiration by nitric oxide induces a Mycobacterium
tuberculosis dormancy program.";
J. Exp. Med. 198:705-713(2003).
[3]
INDUCTION BY CARBON MONOXIDE (CO).
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
Shiloh M.U., Manzanillo P., Cox J.S.;
"Mycobacterium tuberculosis senses host-derived carbon monoxide during
macrophage infection.";
Cell Host Microbe 3:323-330(2008).
[4]
INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18400743; DOI=10.1074/jbc.M802274200;
Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S.,
Kramnik I., Agarwal A., Steyn A.J.;
"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
tuberculosis dormancy regulon.";
J. Biol. Chem. 283:18032-18039(2008).
[5]
PUPYLATION AT LYS-88, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20066036; DOI=10.1371/journal.pone.0008589;
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
Gygi S.P., Darwin K.H.;
"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
tuberculosis.";
PLoS ONE 5:E8589-E8589(2010).
[6]
DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20541977; DOI=10.1016/j.tube.2010.03.013;
Hingley-Wilson S.M., Lougheed K.E., Ferguson K., Leiva S.,
Williams H.D.;
"Individual Mycobacterium tuberculosis universal stress protein
homologues are dispensable in vitro.";
Tuberculosis 90:236-244(2010).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- INDUCTION: A member of the dormancy regulon. Induced in response
to reduced oxygen tension (hypoxia), low levels of nitric oxide
(NO) and carbon monoxide (CO). It is hoped that this regulon will
give insight into the latent, or dormant phase of infection.
{ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:18474359}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal or hypoxic
and normoxic stationary phase growth, nor in mouse- or human-
derived macrophage cell lines. {ECO:0000269|PubMed:20541977}.
-!- SIMILARITY: Belongs to the universal stress protein A family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AL123456; CCP44768.1; -; Genomic_DNA.
PIR; B70758; B70758.
RefSeq; NP_216512.1; NC_000962.3.
RefSeq; WP_003899121.1; NZ_KK339370.1.
ProteinModelPortal; P9WLP1; -.
SMR; P9WLP1; -.
STRING; 83332.Rv1996; -.
PaxDb; P9WLP1; -.
PRIDE; P9WLP1; -.
EnsemblBacteria; CCP44768; CCP44768; Rv1996.
GeneID; 888863; -.
KEGG; mtu:Rv1996; -.
TubercuList; Rv1996; -.
eggNOG; COG0589; LUCA.
OMA; YARWRED; -.
PhylomeDB; P9WLP1; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0006950; P:response to stress; IEA:InterPro.
InterPro; IPR006015; Universal_stress_UspA.
InterPro; IPR006016; UspA.
Pfam; PF00582; Usp; 2.
PRINTS; PR01438; UNVRSLSTRESS.
1: Evidence at protein level;
ATP-binding; Complete proteome; Isopeptide bond; Nucleotide-binding;
Reference proteome; Ubl conjugation.
CHAIN 1 317 Universal stress protein Rv1996.
/FTId=PRO_0000103924.
NP_BIND 128 134 ATP 1. {ECO:0000250|UniProtKB:P9WFD7}.
NP_BIND 142 143 ATP 1. {ECO:0000250|UniProtKB:P9WFD7}.
NP_BIND 277 283 ATP 2. {ECO:0000250|UniProtKB:P9WFD7}.
NP_BIND 291 293 ATP 2. {ECO:0000250|UniProtKB:P9WFD7}.
BINDING 13 13 ATP 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P9WFD7}.
BINDING 175 175 ATP 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P9WFD7}.
BINDING 208 208 ATP 2. {ECO:0000250|UniProtKB:P9WFD7}.
CROSSLNK 88 88 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
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


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