RSEA_MYCS2
ID RSEA_MYCS2 Reviewed; 132 AA.
AC A0R2D3; I7FRJ7;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=MSMEG_5071, MSMEI_4944;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP INTERACTION WITH SIGE, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 700084 / mc(2)155;
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).
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 (By similarity). {ECO:0000250}.
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 ECF RNA polymerase sigma factor SigE,
CC interaction is abrogated by treatment of cells with H(2)O(2), detergent
CC or vancomycin (the latter 2 cause surface stress). This probably
CC inhibits the interaction of SigE with the RNA polymerase catalytic
CC core. {ECO:0000269|PubMed:20025669}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Total levels of RseA decrease after detergent or vancomycin
CC treatment of whole cells (at protein level).
CC {ECO:0000269|PubMed:20025669}.
CC -!- PTM: Phosphorylated by PknB on Thr-36; can be dephosphorylated (at
CC least in vitro) by PstP. Phosphorylation is the signal for subsequent
CC degradation by the ClpC1-ClpP2 complex (By similarity). {ECO:0000250}.
CC -!- PTM: Degraded following vancomycin treatment (surface stress) by a
CC ClpC1-ClpP2 complex. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No phenotype upon growth in liquid culture.
CC {ECO:0000269|PubMed:20025669}.
CC -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP41388.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK72380.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41388.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003896479.1; NZ_SIJM01000019.1.
DR RefSeq; YP_889321.1; NC_008596.1.
DR AlphaFoldDB; A0R2D3; -.
DR SMR; A0R2D3; -.
DR STRING; 246196.MSMEI_4944; -.
DR EnsemblBacteria; ABK72380; ABK72380; MSMEG_5071.
DR EnsemblBacteria; AFP41388; AFP41388; MSMEI_4944.
DR GeneID; 66736391; -.
DR KEGG; msg:MSMEI_4944; -.
DR KEGG; msm:MSMEG_5071; -.
DR PATRIC; fig|246196.19.peg.4949; -.
DR eggNOG; COG5662; Bacteria.
DR OMA; FSWLPSQ; -.
DR OrthoDB; 1902455at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..132
FT /note="Anti-sigma-E factor RseA"
FT /id="PRO_0000422951"
FT REGION 106..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 67
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 MOD_RES 36
FT /note="Phosphothreonine; by PknB"
FT /evidence="ECO:0000250"
SQ SEQUENCE 132 AA; 14426 MW; 8F94510E3C8C5A1B CRC64;
MADPGHVFRR AFSWLPSQFA SQSDAPVGAP RQFGSTEHLS VEAIAAFVDG ELRMSAHLRA
AHHLSLCPEC AAEVDAQSQA RTALRESCPI AIPNSLLGML SQIPHRTPEV TPDVSEQAKF
ADDPTRGRRK RR
