ID   RSLA_MYCTO              Reviewed;         250 AA.
AC   P9WJ66; 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 33.
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=MT0760;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 (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 SigL; this
CC       should inhibit the interaction of SigL with the RNA polymerase
CC       catalytic core. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the zinc-associated anti-sigma factor (ZAS)
CC       superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK44994.1; -; Genomic_DNA.
DR   RefSeq; WP_003403733.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJ66; -.
DR   SMR; P9WJ66; -.
DR   EnsemblBacteria; AAK44994; AAK44994; MT0760.
DR   KEGG; mtc:MT0760; -.
DR   PATRIC; fig|83331.31.peg.814; -.
DR   HOGENOM; CLU_056526_1_0_11; -.
DR   Proteomes; UP000001020; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell membrane; Membrane; Metal-binding; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix; Virulence;
KW   Zinc.
FT   CHAIN           1..250
FT                   /note="Anti-sigma-L factor RslA"
FT                   /id="PRO_0000427883"
FT   TOPO_DOM        1..115
FT                   /note="Cytoplasmic"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..250
FT                   /note="Extracellular"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
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