ID   RSDA_MYCTO              Reviewed;         299 AA.
AC   P9WJ70; L0TFJ3; P65081; Q50713;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
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=MT3522;
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 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       Neither S1P nor S2P proteases have been so far identified for this
CC       anti-sigma factor (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}.
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DR   EMBL; AE000516; AAK47860.1; -; Genomic_DNA.
DR   PIR; B70737; B70737.
DR   RefSeq; WP_003418011.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJ70; -.
DR   SMR; P9WJ70; -.
DR   EnsemblBacteria; AAK47860; AAK47860; MT3522.
DR   KEGG; mtc:MT3522; -.
DR   PATRIC; fig|83331.31.peg.3779; -.
DR   HOGENOM; CLU_059914_0_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   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_0000427881"
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          24..50
FT                   /note="Interaction with sigma factor"
FT                   /evidence="ECO:0000250"
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