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Anti-sigma-L factor RslA (Regulator of SigL) (Sigma-L anti-sigma factor RslA)

 RSLA_MYCTU              Reviewed;         250 AA.
P9WJ67; F2GMW1; Q7ARS0; Q7D9D3;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
15-FEB-2017, entry version 18.
RecName: Full=Anti-sigma-L factor RslA;
AltName: Full=Regulator of SigL;
AltName: Full=Sigma-L anti-sigma factor RslA;
Name=rslA; OrderedLocusNames=Rv0736;
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]
INTERACTION SIGL, INDUCTION, AND TOPOLOGY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16199577; DOI=10.1128/JB.187.20.7062-7071.2005;
Hahn M.Y., Raman S., Anaya M., Husson R.N.;
"The Mycobacterium tuberculosis extracytoplasmic-function sigma factor
SigL regulates polyketide synthases and secreted or membrane proteins
and is required for virulence.";
J. Bacteriol. 187:7062-7071(2005).
[3]
FUNCTION, INTERACTION WITH SIGL, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16552079; DOI=10.1128/IAI.74.4.2457-2461.2006;
Dainese E., Rodrigue S., Delogu G., Provvedi R., Laflamme L.,
Brzezinski R., Fadda G., Smith I., Gaudreau L., Palu G.,
Manganelli R.;
"Posttranslational regulation of Mycobacterium tuberculosis
extracytoplasmic-function sigma factor sigma L and roles in virulence
and in global regulation of gene expression.";
Infect. Immun. 74:2457-2461(2006).
[4]
INTERACTION WITH SIGL.
PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
"Over-expression and purification strategies for recombinant multi-
protein oligomers: a case study of Mycobacterium tuberculosis
sigma/anti-sigma factor protein complexes.";
Protein Expr. Purif. 74:223-230(2010).
[5]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-108 IN COMPLEX WITH ZINC
AND SIGL, SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-54 AND CYS-65.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20184899; DOI=10.1016/j.jmb.2010.02.026;
Thakur K.G., Praveena T., Gopal B.;
"Structural and biochemical bases for the redox sensitivity of
Mycobacterium tuberculosis RslA.";
J. Mol. Biol. 397:1199-1208(2010).
-!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
sigma factor SigL. ECF sigma factors are held in an inactive form
by an anti-sigma factor until released by regulated intramembrane
proteolysis (RIP). RIP occurs when an extracytoplasmic signal
triggers a concerted proteolytic cascade to transmit information
and elicit cellular responses. The membrane-spanning regulatory
substrate protein is first cut extracytoplasmically (site-1
protease, S1P), then within the membrane itself (site-2 protease,
S2P, Rip1), while cytoplasmic proteases finish degrading the
regulatory protein, liberating the sigma factor.
{ECO:0000269|PubMed:16552079}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 Zn(2+) ion per subunit.;
-!- SUBUNIT: Interacts with ECF RNA polymerase sigma factor SigL; this
should inhibit the interaction of SigL with the RNA polymerase
catalytic core. {ECO:0000269|PubMed:16199577,
ECO:0000269|PubMed:16552079, ECO:0000269|PubMed:20184899,
ECO:0000269|PubMed:20600947}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- INDUCTION: Constitutively expressed from a very weak SigL-
independent promoter during growth in culture. Also weakly
autoregulated. Forms an operon with sigL.
{ECO:0000269|PubMed:16199577}.
-!- DOMAIN: The cytosolic domain interacts with sigma factor SigL.
{ECO:0000269|PubMed:20184899}.
-!- DISRUPTION PHENOTYPE: In a double sigL-rslA disruption mutant, no
visible phenotype; not more susceptible than the parental strain
to several oxidative and nitrosative stresses. Infected DBA/2 mice
showed a significantly prolonged survival time relative to mice
infected with wild-type bacteria, although bacteria proliferate
normally. {ECO:0000269|PubMed:16552079}.
-!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP43481.1; -; Genomic_DNA.
RefSeq; NP_215250.1; NC_000962.3.
RefSeq; WP_003403733.1; NZ_KK339370.1.
PDB; 3HUG; X-ray; 2.35 A; B/D/F/H/J/L/N/P/R/T=1-108.
PDBsum; 3HUG; -.
ProteinModelPortal; P9WJ67; -.
SMR; P9WJ67; -.
STRING; 83332.Rv0736; -.
PaxDb; P9WJ67; -.
EnsemblBacteria; CCP43481; CCP43481; Rv0736.
GeneID; 888611; -.
KEGG; mtu:Rv0736; -.
TubercuList; Rv0736; -.
eggNOG; ENOG410600C; Bacteria.
eggNOG; COG5662; LUCA.
OMA; RIDMACS; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
GO; GO:0040007; P:growth; IMP:MTBBASE.
GO; GO:0009405; P:pathogenesis; 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.
InterPro; IPR027383; Znf_put.
Pfam; PF13490; zf-HC2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Membrane;
Metal-binding; Reference proteome; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix;
Virulence; Zinc.
CHAIN 1 250 Anti-sigma-L factor RslA.
/FTId=PRO_0000422682.
TOPO_DOM 1 115 Cytoplasmic.
{ECO:0000269|PubMed:16199577}.
TRANSMEM 116 136 Helical. {ECO:0000255}.
TOPO_DOM 137 250 Extracellular.
{ECO:0000269|PubMed:16199577}.
COMPBIAS 108 114 Poly-Arg.
METAL 25 25 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:20184899}.
METAL 50 50 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:20184899}.
METAL 54 54 Zinc. {ECO:0000269|PubMed:20184899}.
METAL 57 57 Zinc. {ECO:0000269|PubMed:20184899}.
MUTAGEN 54 54 C->S: Loss of Zn(2+)-binding.
{ECO:0000269|PubMed:20184899}.
MUTAGEN 65 65 C->S: No change in Zn(2+)-binding.
{ECO:0000269|PubMed:20184899}.
HELIX 26 30 {ECO:0000244|PDB:3HUG}.
HELIX 31 35 {ECO:0000244|PDB:3HUG}.
HELIX 41 52 {ECO:0000244|PDB:3HUG}.
HELIX 55 64 {ECO:0000244|PDB:3HUG}.
HELIX 67 71 {ECO:0000244|PDB:3HUG}.
HELIX 76 84 {ECO:0000244|PDB:3HUG}.
SEQUENCE 250 AA; 25938 MW; D7FB0253C04F9064 CRC64;
MTMPLRGLGP PDDTGVREVS TGDDHHYAMW DAAYVLGALS AADRREFEAH LAGCPECRGA
VTELCGVPAL LSQLDRDEVA AISESAPTVV ASGLSPELLP SLLAAVHRRR RRTRLITWVA
SSAAAAVLAI GVLVGVQGHS AAPQRAAVSA LPMAQVGTQL LASTVSISGE PWGTFINLRC
VCLAPPYASH DTLAMVVVGR DGSQTRLATW LAEPGHTATP AGSISTPVDQ IAAVQVVAAD
TGQVLLQRSL


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