ID   RSDA_MYCBO              Reviewed;         299 AA.
AC   P65082; A0A1R3Y5T9; Q50713; X2BNM8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=BQ2027_MB3447C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
CC   -!- DOMAIN: The cytosolic domain interacts with ECF sigma factor SigD.
CC       {ECO:0000250}.
CC   -!- PTM: The cytosolic fragment is degraded by a ClpP1-ClpP2-ClpX complex,
CC       as would be expected after S1P and S2P intramembrane proteolysis. This
CC       releases SigD so that it may bind to the RNA polymerase catalytic core
CC       (By similarity). {ECO:0000250}.
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; LT708304; SIU02075.1; -; Genomic_DNA.
DR   RefSeq; NP_857087.1; NC_002945.3.
DR   RefSeq; WP_003418011.1; NC_002945.4.
DR   AlphaFoldDB; P65082; -.
DR   SMR; P65082; -.
DR   EnsemblBacteria; SIU02075; SIU02075; BQ2027_MB3447C.
DR   PATRIC; fig|233413.5.peg.3782; -.
DR   OMA; HAMMFNE; -.
DR   Proteomes; UP000001419; 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_0000104134"
FT   TRANSMEM        86..106
FT                   /note="Helical"
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