RSDA_MYCTU
ID RSDA_MYCTU Reviewed; 299 AA.
AC P9WJ71; 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 32.
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=Rv3413c; ORFNames=MTCY78.16;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15375142; DOI=10.1128/jb.186.19.6605-6616.2004;
RA Raman S., Hazra R., Dascher C.C., Husson R.N.;
RT "Transcription regulation by the Mycobacterium tuberculosis alternative
RT sigma factor SigD and its role in virulence.";
RL J. Bacteriol. 186:6605-6616(2004).
RN [3]
RP INTERACTION WITH SIGMA FACTOR SIGD.
RX PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
RA Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
RT "Over-expression and purification strategies for recombinant multi-protein
RT oligomers: a case study of Mycobacterium tuberculosis sigma/anti-sigma
RT factor protein complexes.";
RL Protein Expr. Purif. 74:223-230(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-80 IN COMPLEX WITH SIGD,
RP INTERACTION WITH SIGD, DOMAIN, CLEAVAGE BY CLP PROTEASE, AND MUTAGENESIS OF
RP TRP-50 AND 93-ALA-ALA-94.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23314154; DOI=10.1093/nar/gks1468;
RA Jaiswal R.K., Prabha T.S., Manjeera G., Gopal B.;
RT "Mycobacterium tuberculosis RsdA provides a conformational rationale for
RT selective regulation of sigma-factor activity by proteolysis.";
RL Nucleic Acids Res. 41:3414-3423(2013).
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.
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:0000269|PubMed:20600947,
CC ECO:0000269|PubMed:23314154}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Positively regulated by alternative sigma factor SigD.
CC {ECO:0000269|PubMed:15375142}.
CC -!- DOMAIN: The cytosolic domain interacts with ECF sigma factor SigD.
CC {ECO:0000269|PubMed:23314154}.
CC -!- PTM: The cytosolic fragment (residues 1-94) in both free and SigD-
CC associated form, is degraded by a ClpP1-ClpP2-ClpX complex, as would be
CC expected after S1P and S2P intramembrane proteolysis. This releases
CC SigD so that it may bind to the RNA polymerase catalytic core.
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DR EMBL; AL123456; CCP46235.1; -; Genomic_DNA.
DR PIR; B70737; B70737.
DR RefSeq; NP_217930.1; NC_000962.3.
DR RefSeq; WP_003418011.1; NZ_NVQJ01000027.1.
DR PDB; 3VEP; X-ray; 2.50 A; C/G/J/X=1-80.
DR PDBsum; 3VEP; -.
DR AlphaFoldDB; P9WJ71; -.
DR SMR; P9WJ71; -.
DR STRING; 83332.Rv3413c; -.
DR PaxDb; P9WJ71; -.
DR DNASU; 887925; -.
DR GeneID; 887925; -.
DR KEGG; mtu:Rv3413c; -.
DR TubercuList; Rv3413c; -.
DR eggNOG; ENOG5033V1E; Bacteria.
DR OMA; HAMMFNE; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..299
FT /note="Anti-sigma-D factor RsdA"
FT /id="PRO_0000104133"
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 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"
FT MUTAGEN 50
FT /note="W->A: 10-fold reduction in binding to SigD."
FT /evidence="ECO:0000269|PubMed:23314154"
FT MUTAGEN 93..94
FT /note="AA->DD: No proteolysis by ClpP1-ClpP2-ClpX."
FT /evidence="ECO:0000269|PubMed:23314154"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:3VEP"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:3VEP"
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
