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Hypoxic response protein 1 (HRP1)

 HRP1_MYCTU              Reviewed;         143 AA.
P9WJA3; L0TBT6; O06186; Q7D6V4;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-JUN-2017, entry version 21.
RecName: Full=Hypoxic response protein 1;
Short=HRP1;
Name=hrp1; OrderedLocusNames=Rv2626c;
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 HYPOXIA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11416222; DOI=10.1073/pnas.121172498;
Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
Schoolnik G.K.;
"Regulation of the Mycobacterium tuberculosis hypoxic response gene
encoding alpha -crystallin.";
Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
[3]
IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY HYPOXIA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12057942; DOI=10.1128/JB.184.13.3485-3491.2002;
Rosenkrands I., Slayden R.A., Crawford J., Aagaard C., Barry C.E. III,
Andersen P.;
"Hypoxic response of Mycobacterium tuberculosis studied by metabolic
labeling and proteome analysis of cellular and extracellular
proteins.";
J. Bacteriol. 184:3485-3491(2002).
[4]
INDUCTION BY NITRIC OXIDE (NO); BY HYPOXIA; IN MOUSE MODEL 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).
[5]
INDUCTION BY HOST IMMUNITY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12506197; DOI=10.1073/pnas.0136863100;
Shi L., Jung Y.J., Tyagi S., Gennaro M.L., North R.J.;
"Expression of Th1-mediated immunity in mouse lungs induces a
Mycobacterium tuberculosis transcription pattern characteristic of
nonreplicating persistence.";
Proc. Natl. Acad. Sci. U.S.A. 100:241-246(2003).
[6]
STATIONARY PHASE INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=S-02293 Harlingen;
PubMed=15528667; DOI=10.1099/mic.0.27284-0;
Starck J., Kallenius G., Marklund B.I., Andersson D.I., Akerlund T.;
"Comparative proteome analysis of Mycobacterium tuberculosis grown
under aerobic and anaerobic conditions.";
Microbiology 150:3821-3829(2004).
[7]
SUBUNIT, AND PRELIMINARY CRYSTALLOGRAPHY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16511097; DOI=10.1107/S1744309105014235;
Sharpe M.L., Baker E.N., Lott J.S.;
"Crystallization of a protein using dehydration without a
precipitant.";
Acta Crystallogr. F 61:565-568(2005).
[8]
BIOTECHNOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17145953; DOI=10.1128/IAI.01137-06;
Roupie V., Romano M., Zhang L., Korf H., Lin M.Y., Franken K.L.,
Ottenhoff T.H., Klein M.R., Huygen K.;
"Immunogenicity of eight dormancy regulon-encoded proteins of
Mycobacterium tuberculosis in DNA-vaccinated and tuberculosis-infected
mice.";
Infect. Immun. 75:941-949(2007).
[9]
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).
[10]
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).
[11]
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).
[12]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-127, SUBUNIT, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF CYS-14; CYS-39 AND CYS-136.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18640126; DOI=10.1016/j.jmb.2008.07.001;
Sharpe M.L., Gao C., Kendall S.L., Baker E.N., Lott J.S.;
"The structure and unusual protein chemistry of hypoxic response
protein 1, a latency antigen and highly expressed member of the DosR
regulon in Mycobacterium tuberculosis.";
J. Mol. Biol. 383:822-836(2008).
-!- FUNCTION: Unlike some other CBS-domain containing proteins does
not seem to bind AMP.
-!- SUBUNIT: Homodimer. Forms an SDS-resistant dimer that requires
Cys-136 for SDS-resistance. {ECO:0000269|PubMed:16511097,
ECO:0000269|PubMed:18640126}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18640126}.
Note=Not seen to be associated with the cell wall.
-!- 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.
Following a shift from stationary to anaerobic growth this protein
is not seen to not be further induced (at protein level). Induced
in mouse lungs at the same time that adaptive host immunity
induces bacterial growth arrest; induction is dependent on
interferon gamma. {ECO:0000269|PubMed:11416222,
ECO:0000269|PubMed:12057942, ECO:0000269|PubMed:12506197,
ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:18400743,
ECO:0000269|PubMed:18474359}.
-!- BIOTECHNOLOGY: In plasmid DNA-vaccinated mice, subsequent
challenge with this protein induces positive levels of antigen-
specific IFN-gamma and IL-2, indicating this might be a good
vaccine candidate. {ECO:0000269|PubMed:17145953}.
-!- MISCELLANEOUS: Has been detected extracellularly but no signal
sequence is predicted by bioinformatic programs.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP45424.1; -; Genomic_DNA.
PIR; A70573; A70573.
RefSeq; NP_217142.1; NC_000962.3.
RefSeq; WP_003413598.1; NZ_KK339370.1.
PDB; 1XKF; X-ray; 1.90 A; A/B=1-127.
PDB; 1Y5H; X-ray; 1.50 A; A/B=1-127.
PDBsum; 1XKF; -.
PDBsum; 1Y5H; -.
ProteinModelPortal; P9WJA3; -.
SMR; P9WJA3; -.
STRING; 83332.Rv2626c; -.
PaxDb; P9WJA3; -.
EnsemblBacteria; CCP45424; CCP45424; Rv2626c.
GeneID; 888576; -.
KEGG; mtu:Rv2626c; -.
TubercuList; Rv2626c; -.
eggNOG; ENOG4107ZWT; Bacteria.
eggNOG; COG0517; LUCA.
OMA; GQYGPLY; -.
PhylomeDB; P9WJA3; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0052553; P:modulation by symbiont of host immune response; IDA:MTBBASE.
GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
InterPro; IPR000644; CBS_dom.
Pfam; PF00571; CBS; 2.
SMART; SM00116; CBS; 2.
PROSITE; PS51371; CBS; 2.
1: Evidence at protein level;
3D-structure; CBS domain; Complete proteome; Disulfide bond;
Metal-binding; Reference proteome; Repeat; Secreted; Zinc.
CHAIN 1 143 Hypoxic response protein 1.
/FTId=PRO_0000392622.
DOMAIN 8 65 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 73 131 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
METAL 97 97 Zinc 1.
METAL 122 122 Zinc 2.
DISULFID 14 39
DISULFID 136 136 Interchain.
MUTAGEN 14 14 C->A: Forms less stable dimer.
{ECO:0000269|PubMed:18640126}.
MUTAGEN 39 39 C->A: Forms less stable dimer.
{ECO:0000269|PubMed:18640126}.
MUTAGEN 128 143 Missing: No longer forms SDS-resistant
dimer.
MUTAGEN 136 136 C->A: No longer forms SDS-resistant
dimer. {ECO:0000269|PubMed:18640126}.
HELIX 4 7 {ECO:0000244|PDB:1Y5H}.
STRAND 8 10 {ECO:0000244|PDB:1Y5H}.
HELIX 21 31 {ECO:0000244|PDB:1Y5H}.
STRAND 34 39 {ECO:0000244|PDB:1Y5H}.
HELIX 41 43 {ECO:0000244|PDB:1Y5H}.
STRAND 44 50 {ECO:0000244|PDB:1Y5H}.
HELIX 51 56 {ECO:0000244|PDB:1Y5H}.
HELIX 59 61 {ECO:0000244|PDB:1Y5H}.
TURN 65 67 {ECO:0000244|PDB:1Y5H}.
HELIX 70 74 {ECO:0000244|PDB:1Y5H}.
HELIX 87 97 {ECO:0000244|PDB:1Y5H}.
STRAND 100 106 {ECO:0000244|PDB:1Y5H}.
STRAND 109 115 {ECO:0000244|PDB:1Y5H}.
HELIX 116 121 {ECO:0000244|PDB:1Y5H}.
SEQUENCE 143 AA; 15518 MW; CF65AA9144341038 CRC64;
MTTARDIMNA GVTCVGEHET LTAAAQYMRE HDIGALPICG DDDRLHGMLT DRDIVIKGLA
AGLDPNTATA GELARDSIYY VDANASIQEM LNVMEEHQVR RVPVISEHRL VGIVTEADIA
RHLPEHAIVQ FVKAICSPMA LAS


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