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Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA)

 RSEA_MYCTU              Reviewed;         154 AA.
L0T905; O06290;
24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
07-JUN-2017, entry version 28.
RecName: Full=Anti-sigma-E factor RseA;
AltName: Full=Regulator of SigE;
AltName: Full=Sigma-E anti-sigma factor RseA;
Name=rseA; OrderedLocusNames=Rv1222;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9139909; DOI=10.1128/jb.179.9.2922-2929.1997;
Wu Q.L., Kong D., Lam K., Husson R.N.;
"A mycobacterial extracytoplasmic function sigma factor involved in
survival following stress.";
J. Bacteriol. 179:2922-2929(1997).
[2]
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).
[3]
FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH SIGE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18606740; DOI=10.1128/JB.00622-08;
Dona V., Rodrigue S., Dainese E., Palu G., Gaudreau L., Manganelli R.,
Provvedi R.;
"Evidence of complex transcriptional, translational, and
posttranslational regulation of the extracytoplasmic function sigma
factor sigmaE in Mycobacterium tuberculosis.";
J. Bacteriol. 190:5963-5971(2008).
[4]
FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH SIGE; CLPC1 AND
CLPX, CLEAVAGE, PHOSPHORYLATION AT THR-39, AND MUTAGENESIS OF THR-39;
CYS-70; CYS-73; THR-98 AND CYS-109.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
"RseA, the SigE specific anti-sigma factor of Mycobacterium
tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2
proteolysis.";
Mol. Microbiol. 75:592-606(2010).
[5]
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).
-!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
sigma factor SigE. ECF sigma factors are held in an inactive form
by an anti-sigma factor. {ECO:0000269|PubMed:18606740,
ECO:0000269|PubMed:20025669}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with cognate ECF RNA polymerase sigma factor
SigE under reducing conditions; this inhibits the interaction of
SigE with the RNA polymerase catalytic core.
{ECO:0000269|PubMed:18606740, ECO:0000269|PubMed:20025669}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- PTM: Phosphorylated by PknB on Thr-39; can be dephosphorylated (at
least in vitro) by PstP. Phosphorylation is the signal for
subsequent degradation by the ClpC1-ClpP2 complex.
{ECO:0000269|PubMed:20025669}.
-!- PTM: Degraded following vancomycin treatment (surface stress) by a
ClpC1-ClpP2 complex.
-!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
superfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC45269.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U87242; AAC45269.1; ALT_INIT; Genomic_DNA.
EMBL; AL123456; CCP43978.1; -; Genomic_DNA.
RefSeq; NP_215738.1; NC_000962.3.
RefSeq; WP_003406258.1; NZ_KK339370.1.
ProteinModelPortal; L0T905; -.
STRING; 83332.Rv1222; -.
iPTMnet; L0T905; -.
PaxDb; L0T905; -.
PRIDE; L0T905; -.
EnsemblBacteria; CCP43978; CCP43978; Rv1222.
GeneID; 885196; -.
KEGG; mtu:Rv1222; -.
TubercuList; Rv1222; -.
eggNOG; ENOG4106684; Bacteria.
eggNOG; ENOG41123YS; LUCA.
OMA; FSWLPSQ; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Metal-binding; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation; Zinc.
CHAIN 1 154 Anti-sigma-E factor RseA.
/FTId=PRO_0000422950.
METAL 66 66 Zinc; via tele nitrogen. {ECO:0000250}.
METAL 70 70 Zinc. {ECO:0000250}.
METAL 73 73 Zinc. {ECO:0000250}.
MOD_RES 39 39 Phosphothreonine; by PknB.
{ECO:0000269|PubMed:20025669}.
MUTAGEN 39 39 T->A: Loss of phosphorylation, no protein
degradation.
{ECO:0000269|PubMed:20025669}.
MUTAGEN 70 70 C->A: Considerably reduced interaction
with SigE. Complete loss of interaction;
when associated with A-73.
{ECO:0000269|PubMed:20025669}.
MUTAGEN 73 73 C->A: Considerably reduced interaction
with SigE. Complete loss of interaction;
when associated with A-70.
{ECO:0000269|PubMed:20025669}.
MUTAGEN 98 98 T->A: No change in phosphorylation.
{ECO:0000269|PubMed:20025669}.
MUTAGEN 109 109 C->A: No change in interaction with SigE.
{ECO:0000269|PubMed:20025669}.
SEQUENCE 154 AA; 16250 MW; 3EED07D9584F06AA CRC64;
MADPGSVGHV FRRAFSWLPA QFASQSDAPV GAPRQFRSTE HLSIEAIAAF VDGELRMNAH
LRAAHHLSLC AQCAAEVDDQ SRARAALRDS HPIRIPSTLL GLLSEIPRCP PEGPSKGSSG
GSSQGPPDGA AAGFGDRFAD GDGGNRGRQS RVRR


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