RSLA_MYCTU
ID RSLA_MYCTU Reviewed; 250 AA.
AC P9WJ67; F2GMW1; Q7ARS0; Q7D9D3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Anti-sigma-L factor RslA;
DE AltName: Full=Regulator of SigL;
DE AltName: Full=Sigma-L anti-sigma factor RslA;
GN Name=rslA; OrderedLocusNames=Rv0736;
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 [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 [2]
RP INTERACTION SIGL, INDUCTION, AND TOPOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16199577; DOI=10.1128/jb.187.20.7062-7071.2005;
RA Hahn M.Y., Raman S., Anaya M., Husson R.N.;
RT "The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL
RT regulates polyketide synthases and secreted or membrane proteins and is
RT required for virulence.";
RL J. Bacteriol. 187:7062-7071(2005).
RN [3]
RP FUNCTION, INTERACTION WITH SIGL, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16552079; DOI=10.1128/iai.74.4.2457-2461.2006;
RA Dainese E., Rodrigue S., Delogu G., Provvedi R., Laflamme L.,
RA Brzezinski R., Fadda G., Smith I., Gaudreau L., Palu G., Manganelli R.;
RT "Posttranslational regulation of Mycobacterium tuberculosis
RT extracytoplasmic-function sigma factor sigma L and roles in virulence and
RT in global regulation of gene expression.";
RL Infect. Immun. 74:2457-2461(2006).
RN [4]
RP INTERACTION WITH SIGL.
RX PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
RA Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
RT "Over-expression and purification strategies for recombinant multi-protein
RT oligomers: a case study of Mycobacterium tuberculosis sigma/anti-sigma
RT factor protein complexes.";
RL Protein Expr. Purif. 74:223-230(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-108 IN COMPLEX WITH ZINC AND
RP SIGL, SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-54 AND CYS-65.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20184899; DOI=10.1016/j.jmb.2010.02.026;
RA Thakur K.G., Praveena T., Gopal B.;
RT "Structural and biochemical bases for the redox sensitivity of
RT Mycobacterium tuberculosis RslA.";
RL J. Mol. Biol. 397:1199-1208(2010).
CC -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC sigma factor SigL. ECF sigma factors are held in an inactive form by an
CC anti-sigma factor until released by regulated intramembrane proteolysis
CC (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted
CC proteolytic cascade to transmit information and elicit cellular
CC responses. The membrane-spanning regulatory substrate protein is first
CC cut extracytoplasmically (site-1 protease, S1P), then within the
CC membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic
CC proteases finish degrading the regulatory protein, liberating the sigma
CC factor. {ECO:0000269|PubMed:16552079}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 Zn(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts with ECF RNA polymerase sigma factor SigL; this
CC should inhibit the interaction of SigL with the RNA polymerase
CC catalytic core. {ECO:0000269|PubMed:16199577,
CC ECO:0000269|PubMed:16552079, ECO:0000269|PubMed:20184899,
CC ECO:0000269|PubMed:20600947}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed from a very weak SigL-independent
CC promoter during growth in culture. Also weakly autoregulated. Forms an
CC operon with sigL. {ECO:0000269|PubMed:16199577}.
CC -!- DOMAIN: The cytosolic domain interacts with sigma factor SigL.
CC {ECO:0000269|PubMed:20184899}.
CC -!- DISRUPTION PHENOTYPE: In a double sigL-rslA disruption mutant, no
CC visible phenotype; not more susceptible than the parental strain to
CC several oxidative and nitrosative stresses. Infected DBA/2 mice showed
CC a significantly prolonged survival time relative to mice infected with
CC wild-type bacteria, although bacteria proliferate normally.
CC {ECO:0000269|PubMed:16552079}.
CC -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP43481.1; -; Genomic_DNA.
DR RefSeq; NP_215250.1; NC_000962.3.
DR RefSeq; WP_003403733.1; NZ_NVQJ01000007.1.
DR PDB; 3HUG; X-ray; 2.35 A; B/D/F/H/J/L/N/P/R/T=1-108.
DR PDBsum; 3HUG; -.
DR AlphaFoldDB; P9WJ67; -.
DR SMR; P9WJ67; -.
DR STRING; 83332.Rv0736; -.
DR PaxDb; P9WJ67; -.
DR DNASU; 888611; -.
DR GeneID; 888611; -.
DR KEGG; mtu:Rv0736; -.
DR TubercuList; Rv0736; -.
DR eggNOG; COG1595; Bacteria.
DR OMA; RIDMACS; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR Gene3D; 1.10.10.1320; -; 1.
DR InterPro; IPR041916; Anti_sigma_zinc_sf.
DR InterPro; IPR027383; Znf_put.
DR Pfam; PF13490; zf-HC2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Virulence; Zinc.
FT CHAIN 1..250
FT /note="Anti-sigma-L factor RslA"
FT /id="PRO_0000422682"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16199577"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..250
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16199577"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20184899"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20184899"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20184899"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20184899"
FT MUTAGEN 54
FT /note="C->S: Loss of Zn(2+)-binding."
FT /evidence="ECO:0000269|PubMed:20184899"
FT MUTAGEN 65
FT /note="C->S: No change in Zn(2+)-binding."
FT /evidence="ECO:0000269|PubMed:20184899"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:3HUG"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3HUG"
SQ 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
