Y2005_MYCTU
ID Y2005_MYCTU Reviewed; 295 AA.
AC P9WLN1; 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 38.
DE RecName: Full=Universal stress protein Rv2005c;
DE Short=USP Rv2005c;
GN OrderedLocusNames=Rv2005c; ORFNames=MTCY39.12;
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 HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [3]
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 [4]
RP INDUCTION BY ANAEROBISIS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=S-02293 Harlingen;
RX PubMed=15528667; DOI=10.1099/mic.0.27284-0;
RA Starck J., Kallenius G., Marklund B.I., Andersson D.I., Akerlund T.;
RT "Comparative proteome analysis of Mycobacterium tuberculosis grown under
RT aerobic and anaerobic conditions.";
RL Microbiology 150:3821-3829(2004).
RN [5]
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 [6]
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 [7]
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 [8]
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=31059757; DOI=10.1016/j.micpath.2019.05.001;
RA Sharma D., Lata M., Faheem M., Khan A.U., Joshi B., Venkatesan K.,
RA Shukla S., Bisht D.;
RT "Role of M.tuberculosis protein Rv2005c in the aminoglycosides
RT resistance.";
RL Microb. Pathog. 132:150-155(2019).
CC -!- FUNCTION: Probably involved in aminoglycosides resistance and
CC virulence. Overexpression increases resistance to the aminoglycosides
CC amikacin (AK) and kanamycin (KM). {ECO:0000269|PubMed:31059757}.
CC -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC reduced oxygen tension (hypoxia) (at protein level), low levels of
CC nitric oxide (NO) and carbon monoxide (CO). It is hoped that this
CC regulon will give insight into the latent, or dormant phase of
CC infection. {ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12953092,
CC ECO:0000269|PubMed:15528667, 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; CCP44777.1; -; Genomic_DNA.
DR PIR; C70759; C70759.
DR RefSeq; NP_216521.1; NC_000962.3.
DR RefSeq; WP_003410060.1; NZ_NVQJ01000043.1.
DR AlphaFoldDB; P9WLN1; -.
DR SMR; P9WLN1; -.
DR STRING; 83332.Rv2005c; -.
DR PaxDb; P9WLN1; -.
DR DNASU; 888831; -.
DR GeneID; 888831; -.
DR KEGG; mtu:Rv2005c; -.
DR TubercuList; Rv2005c; -.
DR eggNOG; COG0589; Bacteria.
DR OMA; TWAVWQE; -.
DR PhylomeDB; P9WLN1; -.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
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 Antibiotic resistance; ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..295
FT /note="Universal stress protein Rv2005c"
FT /id="PRO_0000103934"
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
