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Anti-sigma-D factor RsdA (Regulator of SigD) (Sigma-D anti-sigma factor RsdA)

 RSDA_MYCTU              Reviewed;         299 AA.
P9WJ71; L0TFJ3; P65081; Q50713;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-JUN-2017, entry version 19.
RecName: Full=Anti-sigma-D factor RsdA;
AltName: Full=Regulator of SigD;
AltName: Full=Sigma-D anti-sigma factor RsdA;
Name=rsdA; OrderedLocusNames=Rv3413c; ORFNames=MTCY78.16;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15375142; DOI=10.1128/JB.186.19.6605-6616.2004;
Raman S., Hazra R., Dascher C.C., Husson R.N.;
"Transcription regulation by the Mycobacterium tuberculosis
alternative sigma factor SigD and its role in virulence.";
J. Bacteriol. 186:6605-6616(2004).
[3]
INTERACTION WITH SIGMA FACTOR SIGD.
PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
"Over-expression and purification strategies for recombinant multi-
protein oligomers: a case study of Mycobacterium tuberculosis
sigma/anti-sigma factor protein complexes.";
Protein Expr. Purif. 74:223-230(2010).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[5]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-80 IN COMPLEX WITH SIGD,
INTERACTION WITH SIGD, DOMAIN, CLEAVAGE BY CLP PROTEASE, AND
MUTAGENESIS OF TRP-50 AND 93-ALA-ALA-94.
STRAIN=ATCC 25618 / H37Rv;
PubMed=23314154; DOI=10.1093/nar/gks1468;
Jaiswal R.K., Prabha T.S., Manjeera G., Gopal B.;
"Mycobacterium tuberculosis RsdA provides a conformational rationale
for selective regulation of sigma-factor activity by proteolysis.";
Nucleic Acids Res. 41:3414-3423(2013).
-!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
sigma factor SigD. ECF sigma factors are held in an inactive form
by an anti-sigma factor until released by regulated intramembrane
proteolysis (RIP). RIP occurs when an extracytoplasmic signal
triggers a concerted proteolytic cascade to transmit information
and elicit cellular responses. The membrane-spanning regulatory
substrate protein is first cut extracytoplasmically (site-1
protease, S1P), then within the membrane itself (site-2 protease,
S2P), while cytoplasmic proteases finish degrading the regulatory
protein, liberating the sigma factor. Neither S1P nor S2P
proteases have been so far identified for this anti-sigma factor.
-!- SUBUNIT: Interacts with ECF RNA polymerase sigma factor SigD; this
should inhibit the interaction of SigD with the RNA polymerase
catalytic core. {ECO:0000269|PubMed:20600947,
ECO:0000269|PubMed:23314154}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- INDUCTION: Positively regulated by alternative sigma factor SigD.
{ECO:0000269|PubMed:15375142}.
-!- DOMAIN: The cytosolic domain interacts with ECF sigma factor SigD.
{ECO:0000269|PubMed:23314154}.
-!- PTM: The cytosolic fragment (residues 1-94) in both free and SigD-
associated form, is degraded by a ClpP1-ClpP2-ClpX complex, as
would be expected after S1P and S2P intramembrane proteolysis.
This releases SigD so that it may bind to the RNA polymerase
catalytic core.
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EMBL; AL123456; CCP46235.1; -; Genomic_DNA.
PIR; B70737; B70737.
RefSeq; NP_217930.1; NC_000962.3.
RefSeq; WP_003418011.1; NZ_KK339370.1.
PDB; 3VEP; X-ray; 2.50 A; C/G/J/X=1-80.
PDBsum; 3VEP; -.
ProteinModelPortal; P9WJ71; -.
SMR; P9WJ71; -.
STRING; 83332.Rv3413c; -.
PaxDb; P9WJ71; -.
EnsemblBacteria; CCP46235; CCP46235; Rv3413c.
GeneID; 887925; -.
KEGG; mtu:Rv3413c; -.
TubercuList; Rv3413c; -.
OMA; EPTITMV; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR031928; RsdA_SigD-bd.
Pfam; PF16751; RsdA_SigD_bd; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Membrane;
Reference proteome; Transcription; Transcription regulation;
Transmembrane; Transmembrane helix.
CHAIN 1 299 Anti-sigma-D factor RsdA.
/FTId=PRO_0000104133.
TOPO_DOM 1 85 Cytoplasmic. {ECO:0000255}.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TOPO_DOM 107 299 Extracellular. {ECO:0000255}.
REGION 24 50 Interaction with sigma factor.
COMPBIAS 201 297 Pro-rich.
MUTAGEN 50 50 W->A: 10-fold reduction in binding to
SigD. {ECO:0000269|PubMed:23314154}.
MUTAGEN 93 94 AA->DD: No proteolysis by ClpP1-ClpP2-
ClpX. {ECO:0000269|PubMed:23314154}.
HELIX 13 28 {ECO:0000244|PDB:3VEP}.
HELIX 38 55 {ECO:0000244|PDB:3VEP}.
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


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