ID   RSDA_MYCTE              Reviewed;         299 AA.
AC   H8EZ77;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Anti-sigma-D factor RsdA;
DE   AltName: Full=Regulator of SigD;
DE   AltName: Full=Sigma-D anti-sigma factor RsdA;
GN   Name=rsdA; OrderedLocusNames=ERDMAN_3734;
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   NOT A SUBSTRATE FOR 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 SigD. 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), while cytoplasmic proteases
CC       finish degrading the regulatory protein, liberating the sigma factor
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ECF RNA polymerase sigma factor SigD; this
CC       should inhibit the interaction of SigD 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 SigD.
CC       {ECO:0000250}.
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DR   EMBL; AP012340; BAL67507.1; -; Genomic_DNA.
DR   RefSeq; WP_003418011.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8EZ77; -.
DR   SMR; H8EZ77; -.
DR   EnsemblBacteria; BAL67507; BAL67507; ERDMAN_3734.
DR   KEGG; mtn:ERDMAN_3734; -.
DR   PATRIC; fig|652616.3.peg.3804; -.
DR   HOGENOM; CLU_059914_0_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   InterPro; IPR031928; RsdA_SigD-bd.
DR   Pfam; PF16751; RsdA_SigD_bd; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transcription; Transcription regulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..299
FT                   /note="Anti-sigma-D factor RsdA"
FT                   /id="PRO_0000422681"
FT   TOPO_DOM        1..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          187..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   299 AA;  31248 MW;  CFCEDFE38C8E0B5C CRC64;
     MREFGNPLGD RPPLDELART DLLLDALAER EEVDFADPRD DALAALLGQW RDDLRWPPAS
     ALVSQDEAVA ALRAGVAQRR RARRSLAAVG SVAAALLVLS GFGAVVADAR PGDLLYGLHA
     MMFNRSRVSD DQIVLSAKAN LAKVEQMIAQ GQWAEAQDEL AEVSSTVQAV TDGSRRQDLI
     NEVNLLNTKV ETRDPNATLR PGSPSNPAAP GSVGNSWTPL APVVEPPTPP TPASAAEPSM
     SAGVSESPMP NSTSTVAASP STPSSKPEPG SIDPSLEPAD EATNPAGQPA PETPVSPTH