ID   RSLA_MYCTE              Reviewed;         250 AA.
AC   H8EXN2;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 40.
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=ERDMAN_0809;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   POSSIBLE CLEAVAGE BY RIP1.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA   Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT   "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT   three anti-sigma factor substrates.";
RL   Mol. Microbiol. 77:605-617(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 (Probable). {ECO:0000305}.
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   -!- DOMAIN: The cytosolic domain interacts with sigma factor SigL.
CC       {ECO:0000305}.
CC   -!- PTM: Probably cleaved within the membrane by Rip1 near the cytoplasmic
CC       membrane interface.
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DR   EMBL; AP012340; BAL64621.1; -; Genomic_DNA.
DR   RefSeq; WP_003403733.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8EXN2; -.
DR   SMR; H8EXN2; -.
DR   EnsemblBacteria; BAL64621; BAL64621; ERDMAN_0809.
DR   KEGG; mtn:ERDMAN_0809; -.
DR   PATRIC; fig|652616.3.peg.820; -.
DR   HOGENOM; CLU_056526_1_0_11; -.
DR   Proteomes; UP000007568; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell membrane; Membrane; Transcription; Transcription regulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..250
FT                   /note="Anti-sigma-L factor RslA"
FT                   /id="PRO_0000422683"
FT   TOPO_DOM        1..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        137..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
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