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Nucleoid-associated protein EspR (ESX-1 transcriptional regulatory protein EspR)

 ESPR_MYCTU              Reviewed;         132 AA.
P9WJB7; L0TDR1; P96228; Q8VIS2;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
23-MAY-2018, entry version 25.
RecName: Full=Nucleoid-associated protein EspR {ECO:0000305};
AltName: Full=ESX-1 transcriptional regulatory protein EspR {ECO:0000305};
Name=espR; OrderedLocusNames=Rv3849;
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]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[3]
FUNCTION AS AN ACTIVATOR, INDUCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
PubMed=18685700; DOI=10.1038/nature07219;
Raghavan S., Manzanillo P., Chan K., Dovey C., Cox J.S.;
"Secreted transcription factor controls Mycobacterium tuberculosis
virulence.";
Nature 454:717-721(2008).
[4]
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).
[5]
FUNCTION IN REGULATION OF THE ESPACD OPERON.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22389481; DOI=10.1128/JB.00142-12;
Hunt D.M., Sweeney N.P., Mori L., Whalan R.H., Comas I., Norman L.,
Cortes T., Arnvig K.B., Davis E.O., Stapleton M.R., Green J.,
Buxton R.S.;
"Long-range transcriptional control of an operon necessary for
virulence-critical ESX-1 secretion in Mycobacterium tuberculosis.";
J. Bacteriol. 194:2307-2320(2012).
[6]
FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22479184; DOI=10.1371/journal.ppat.1002621;
Blasco B., Chen J.M., Hartkoorn R., Sala C., Uplekar S., Rougemont J.,
Pojer F., Cole S.T.;
"Virulence regulator EspR of Mycobacterium tuberculosis is a nucleoid-
associated protein.";
PLoS Pathog. 8:E1002621-E1002621(2012).
[7]
FUNCTION, AND DNA-BINDING.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=23743602; DOI=10.1007/s00284-013-0404-8;
Cao G., Howard S.T., Zhang P., Hou G., Pang X.;
"Functional analysis of the EspR binding sites upstream of espR in
Mycobacterium tuberculosis.";
Curr. Microbiol. 67:572-579(2013).
[8]
MUTAGENESIS OF ARG-69; LYS-71; ARG-100; ARG-105; ASP-122; ARG-125 AND
ASP-131.
STRAIN=H37Rv;
PubMed=24633871; DOI=10.1128/JB.00039-14;
Blasco B., Japaridze A., Stenta M., Wicky B.I., Dietler G.,
Dal Peraro M., Pojer F., Cole S.T.;
"Functional dissection of intersubunit interactions in the EspR
virulence regulator of Mycobacterium tuberculosis.";
J. Bacteriol. 196:1889-1900(2014).
[9]
INDUCTION.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=25536998; DOI=10.1099/mic.0.000023;
Cao G., Howard S.T., Zhang P., Wang X., Chen X.L., Samten B., Pang X.;
"EspR, a regulator of the ESX-1 secretion system in Mycobacterium
tuberculosis, is directly regulated by the two-component systems MprAB
and PhoPR.";
Microbiology 161:477-489(2015).
[10]
CRYSTALLIZATION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=21206031; DOI=10.1107/S174430911004618X;
Gangwar S.P., Meena S.R., Saxena A.K.;
"Cloning, purification, crystallization and preliminary X-ray analysis
of ESX-1-secreted protein regulator (EspR) from Mycobacterium
tuberculosis.";
Acta Crystallogr. F 67:83-86(2011).
[11] {ECO:0000244|PDB:3QF3, ECO:0000244|PDB:3QWG, ECO:0000244|PDB:3QYX}
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 2-122, FUNCTION,
DNA-BINDING, SUBUNIT, AND DOMAIN.
STRAIN=ATCC 25618 / H37Rv;
PubMed=21883526; DOI=10.1111/j.1365-2958.2011.07813.x;
Blasco B., Stenta M., Alonso-Sarduy L., Dietler G., Peraro M.D.,
Cole S.T., Pojer F.;
"Atypical DNA recognition mechanism used by the EspR virulence
regulator of Mycobacterium tuberculosis.";
Mol. Microbiol. 82:251-264(2011).
[12] {ECO:0000244|PDB:3R1F}
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, DOMAIN, AND
DNA-BINDING.
PubMed=21795602; DOI=10.1073/pnas.1110242108;
Rosenberg O.S., Dovey C., Tempesta M., Robbins R.A., Finer-Moore J.S.,
Stroud R.M., Cox J.S.;
"EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts
a unique dimeric structure among helix-turn-helix proteins.";
Proc. Natl. Acad. Sci. U.S.A. 108:13450-13455(2011).
[13] {ECO:0000244|PDB:4NDW}
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS).
PubMed=24699733; DOI=10.1107/S2053230X14004166;
Gangwar S.P., Meena S.R., Saxena A.K.;
"Comparison of four different crystal forms of the Mycobacterium
tuberculosis ESX-1 secreted protein regulator EspR.";
Acta Crystallogr. F Struct. Biol. Commun. 70:433-437(2014).
-!- FUNCTION: Virulence regulator that has both architectural and
regulatory roles. Impacts cell wall functions and pathogenesis
through regulation of multiple genes, including the espACD operon,
which is a key ESX-1 component. Influences target gene expression
positively or negatively, depending on its binding position
relative to the genes it controls. Acts by binding directly to the
DNA. May play a central role in regulating virulence gene
expression. {ECO:0000269|PubMed:18685700,
ECO:0000269|PubMed:21883526, ECO:0000269|PubMed:22389481,
ECO:0000269|PubMed:22479184, ECO:0000269|PubMed:23743602}.
-!- SUBUNIT: Homodimer. Binds DNA as a dimer of dimers.
{ECO:0000269|PubMed:21795602, ECO:0000269|PubMed:21883526}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-15937970, EBI-15937970;
-!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
{ECO:0000269|PubMed:22479184}.
-!- INDUCTION: Negatively autoregulated (PubMed:22479184).
Transcriptionally regulated by the MprB/MprA and PhoP/PhoR two-
component systems (PubMed:25536998). Expression is growth phase-
dependent, peaking in the stationary phase (PubMed:22479184).
Probably induced upon phagocytosis (PubMed:18685700).
{ECO:0000269|PubMed:18685700, ECO:0000269|PubMed:22479184,
ECO:0000269|PubMed:25536998}.
-!- DOMAIN: The N-terminal domain binds DNA and the C-terminal domain
is involved in dimerization. Both domains are required for
transcriptional activity and for ESX-1 function.
{ECO:0000269|PubMed:18685700, ECO:0000269|PubMed:21795602,
ECO:0000269|PubMed:21883526}.
-!- DISRUPTION PHENOTYPE: Mutants exhibit growth defect during
infection of mice. They establish a stable infection by three
weeks, but the bacterial burden is an order of magnitude less than
the wild-type. {ECO:0000269|PubMed:18685700}.
-!- CAUTION: Was originally thought to be secreted via the ESX-1
secretion system, but it was probably released in the medium via
cell lysis. {ECO:0000305|PubMed:18685700,
ECO:0000305|PubMed:22479184}.
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EMBL; AL123456; CCP46678.1; -; Genomic_DNA.
PIR; F70654; F70654.
RefSeq; NP_218366.1; NC_000962.3.
RefSeq; WP_003399759.1; NZ_KK339374.1.
PDB; 3QF3; X-ray; 2.41 A; A/B/C/D/E/F=2-132.
PDB; 3QWG; X-ray; 1.99 A; A/B=2-122.
PDB; 3QYX; X-ray; 3.75 A; A/B/C/D=2-132.
PDB; 3R1F; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-132.
PDB; 4NDW; X-ray; 3.30 A; A/B=1-132.
PDBsum; 3QF3; -.
PDBsum; 3QWG; -.
PDBsum; 3QYX; -.
PDBsum; 3R1F; -.
PDBsum; 4NDW; -.
ProteinModelPortal; P9WJB7; -.
SMR; P9WJB7; -.
STRING; 83332.Rv3849; -.
PaxDb; P9WJB7; -.
PRIDE; P9WJB7; -.
EnsemblBacteria; CCP46678; CCP46678; Rv3849.
GeneID; 886184; -.
KEGG; mtu:Rv3849; -.
TubercuList; Rv3849; -.
eggNOG; ENOG4105S82; Bacteria.
eggNOG; ENOG4111UCP; LUCA.
OMA; FFTDDDY; -.
Proteomes; UP000001584; Chromosome.
CollecTF; EXPREG_00000c30; -.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0050708; P:regulation of protein secretion; IDA:MTBBASE.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Cytoplasm; DNA-binding;
Reference proteome; Repressor; Transcription;
Transcription regulation; Virulence.
CHAIN 1 132 Nucleoid-associated protein EspR.
/FTId=PRO_0000393905.
DNA_BIND 38 50 H-T-H motif. {ECO:0000255}.
MUTAGEN 69 69 R->A: Affects protein stability.
Decreases affinity for DNA and
dimerization capacity.
{ECO:0000269|PubMed:24633871}.
MUTAGEN 71 71 K->A: Decreases affinity for DNA. Does
not affect dimerization.
{ECO:0000269|PubMed:24633871}.
MUTAGEN 100 100 R->A: Affects protein stability.
Decreases affinity for DNA. Does not
affect dimerization.
{ECO:0000269|PubMed:24633871}.
MUTAGEN 105 105 R->A: Does not affect DNA binding.
{ECO:0000269|PubMed:24633871}.
MUTAGEN 122 122 D->A: Moderate impact on protein
stability. Does not affect DNA binding.
{ECO:0000269|PubMed:24633871}.
MUTAGEN 125 125 R->A: Moderate impact on protein
stability. Does not affect DNA binding.
{ECO:0000269|PubMed:24633871}.
MUTAGEN 131 131 D->A: Moderate impact on protein
stability. Does not affect DNA binding.
{ECO:0000269|PubMed:24633871}.
HELIX 5 15 {ECO:0000244|PDB:3QWG}.
TURN 19 21 {ECO:0000244|PDB:3QWG}.
HELIX 26 35 {ECO:0000244|PDB:3QWG}.
HELIX 42 49 {ECO:0000244|PDB:3QWG}.
STRAND 51 53 {ECO:0000244|PDB:3QF3}.
HELIX 58 67 {ECO:0000244|PDB:3QWG}.
HELIX 73 76 {ECO:0000244|PDB:3QWG}.
HELIX 78 94 {ECO:0000244|PDB:3QWG}.
HELIX 97 106 {ECO:0000244|PDB:3QF3}.
HELIX 111 127 {ECO:0000244|PDB:3QF3}.
SEQUENCE 132 AA; 14709 MW; 84EA0DB906D81996 CRC64;
MSTTFAARLN RLFDTVYPPG RGPHTSAEVI AALKAEGITM SAPYLSQLRS GNRTNPSGAT
MAALANFFRI KAAYFTDDEY YEKLDKELQW LCTMRDDGVR RIAQRAHGLP SAAQQKVLDR
IDELRRAEGI DA


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