RSEA_MYCTU
ID RSEA_MYCTU Reviewed; 154 AA.
AC L0T905; O06290;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Anti-sigma-E factor RseA;
DE AltName: Full=Regulator of SigE;
DE AltName: Full=Sigma-E anti-sigma factor RseA;
GN Name=rseA; OrderedLocusNames=Rv1222;
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 [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9139909; DOI=10.1128/jb.179.9.2922-2929.1997;
RA Wu Q.L., Kong D., Lam K., Husson R.N.;
RT "A mycobacterial extracytoplasmic function sigma factor involved in
RT survival following stress.";
RL J. Bacteriol. 179:2922-2929(1997).
RN [2]
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 [3]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, AND INTERACTION WITH SIGE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18606740; DOI=10.1128/jb.00622-08;
RA Dona V., Rodrigue S., Dainese E., Palu G., Gaudreau L., Manganelli R.,
RA Provvedi R.;
RT "Evidence of complex transcriptional, translational, and posttranslational
RT regulation of the extracytoplasmic function sigma factor sigmaE in
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 190:5963-5971(2008).
RN [4]
RP FUNCTION AS AN ANTI-SIGMA FACTOR, INTERACTION WITH SIGE; CLPC1 AND CLPX,
RP CLEAVAGE, PHOSPHORYLATION AT THR-39, AND MUTAGENESIS OF THR-39; CYS-70;
RP CYS-73; THR-98 AND CYS-109.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20025669; DOI=10.1111/j.1365-2958.2009.07008.x;
RA Barik S., Sureka K., Mukherjee P., Basu J., Kundu M.;
RT "RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis,
RT is inactivated by phosphorylation-dependent ClpC1P2 proteolysis.";
RL Mol. Microbiol. 75:592-606(2010).
RN [5]
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).
CC -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC sigma factor SigE. ECF sigma factors are held in an inactive form by an
CC anti-sigma factor. {ECO:0000269|PubMed:18606740,
CC ECO:0000269|PubMed:20025669}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with cognate ECF RNA polymerase sigma factor SigE
CC under reducing conditions; this inhibits the interaction of SigE with
CC the RNA polymerase catalytic core. {ECO:0000269|PubMed:18606740,
CC ECO:0000269|PubMed:20025669}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by PknB on Thr-39; can be dephosphorylated (at
CC least in vitro) by PstP. Phosphorylation is the signal for subsequent
CC degradation by the ClpC1-ClpP2 complex. {ECO:0000269|PubMed:20025669}.
CC -!- PTM: Degraded following vancomycin treatment (surface stress) by a
CC ClpC1-ClpP2 complex.
CC -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC45269.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U87242; AAC45269.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL123456; CCP43978.1; -; Genomic_DNA.
DR RefSeq; NP_215738.1; NC_000962.3.
DR RefSeq; WP_003406258.1; NZ_NVQJ01000039.1.
DR AlphaFoldDB; L0T905; -.
DR SMR; L0T905; -.
DR STRING; 83332.Rv1222; -.
DR iPTMnet; L0T905; -.
DR PaxDb; L0T905; -.
DR GeneID; 885196; -.
DR KEGG; mtu:Rv1222; -.
DR TubercuList; Rv1222; -.
DR eggNOG; COG5662; Bacteria.
DR OMA; FSWLPSQ; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043856; F:anti-sigma factor antagonist activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
DR Gene3D; 1.10.10.1320; -; 1.
DR InterPro; IPR041916; Anti_sigma_zinc_sf.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..154
FT /note="Anti-sigma-E factor RseA"
FT /id="PRO_0000422950"
FT REGION 104..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphothreonine; by PknB"
FT /evidence="ECO:0000269|PubMed:20025669"
FT MUTAGEN 39
FT /note="T->A: Loss of phosphorylation, no protein
FT degradation."
FT /evidence="ECO:0000269|PubMed:20025669"
FT MUTAGEN 70
FT /note="C->A: Considerably reduced interaction with SigE.
FT Complete loss of interaction; when associated with A-73."
FT /evidence="ECO:0000269|PubMed:20025669"
FT MUTAGEN 73
FT /note="C->A: Considerably reduced interaction with SigE.
FT Complete loss of interaction; when associated with A-70."
FT /evidence="ECO:0000269|PubMed:20025669"
FT MUTAGEN 98
FT /note="T->A: No change in phosphorylation."
FT /evidence="ECO:0000269|PubMed:20025669"
FT MUTAGEN 109
FT /note="C->A: No change in interaction with SigE."
FT /evidence="ECO:0000269|PubMed:20025669"
SQ SEQUENCE 154 AA; 16250 MW; 3EED07D9584F06AA CRC64;
MADPGSVGHV FRRAFSWLPA QFASQSDAPV GAPRQFRSTE HLSIEAIAAF VDGELRMNAH
LRAAHHLSLC AQCAAEVDDQ SRARAALRDS HPIRIPSTLL GLLSEIPRCP PEGPSKGSSG
GSSQGPPDGA AAGFGDRFAD GDGGNRGRQS RVRR
