SIGK_MYCTU
ID SIGK_MYCTU Reviewed; 187 AA.
AC P9WGH7; L0T3R3; O53730; Q7D9T3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=ECF RNA polymerase sigma factor SigK;
DE Short=ECF sigma factor SigK;
DE AltName: Full=Alternative RNA polymerase sigma factor SigK;
DE AltName: Full=RNA polymerase sigma-K factor;
DE Short=Sigma-K factor;
GN Name=sigK; OrderedLocusNames=Rv0445c;
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 FUNCTION AS A SIGMA-FACTOR, AND INDUCTION.
RX PubMed=15882422; DOI=10.1111/j.1365-2958.2005.04618.x;
RA Charlet D., Mostowy S., Alexander D., Sit L., Wiker H.G., Behr M.A.;
RT "Reduced expression of antigenic proteins MPB70 and MPB83 in Mycobacterium
RT bovis BCG strains due to a start codon mutation in sigK.";
RL Mol. Microbiol. 56:1302-1313(2005).
RN [3]
RP INTERACTION WITH RSKA.
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 (2.4 ANGSTROMS) IN COMPLEX WITH RSKA, AND SUBUNIT.
RA Shukla J.K., Gopal B.;
RT "Structure of extra-cytoplasmic function (ECF) sigma factor SigK in complex
RT with its negative regulator RskA from Mycobacterium tuberculosis.";
RL Submitted (JAN-2013) to the PDB data bank.
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. Extracytoplasmic function (ECF) sigma factors are held in an
CC inactive form by an anti-sigma factor until released by regulated
CC intramembrane proteolysis. Sigma-K controls genes such as mpt70 and
CC mpt83. {ECO:0000269|PubMed:15882422}.
CC -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core
CC formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1
CC omega subunit) to form the RNA polymerase holoenzyme that can initiate
CC transcription. Interacts (via sigma-70 factor domain 4) with anti-
CC sigma-K factor RskA. {ECO:0000269|PubMed:20600947, ECO:0000269|Ref.5}.
CC -!- INDUCTION: Autoregulated. {ECO:0000269|PubMed:15882422}.
CC -!- DOMAIN: The sigma-70 factor domain-2 mediates sequence-specific
CC interaction with the -10 element in promoter DNA, and plays an
CC important role in melting the double-stranded DNA and the formation of
CC the transcription bubble. The sigma-70 factor domain-2 mediates
CC interaction with the RNA polymerase subunits RpoB and RpoC (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-
CC H) motif that mediates interaction with the -35 element in promoter
CC DNA. The domain also mediates interaction with the RNA polymerase
CC subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-
CC sigma factors prevents interaction of sigma factors with the RNA
CC polymerase catalytic core (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Extracytoplasmic function (ECF) sigma factors are held
CC in an inactive form by an anti-sigma factor until released by regulated
CC intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic
CC signal triggers a concerted proteolytic cascade to transmit information
CC and elicit cellular responses. The membrane-spanning anti-sigma factor
CC is first cut extracytoplasmically (site-1 protease, S1P), then within
CC the membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic
CC proteases finish degrading the regulatory protein, liberating SigK
CC (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.
CC {ECO:0000305}.
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; AL123456; CCP43176.1; -; Genomic_DNA.
DR PIR; F70830; F70830.
DR RefSeq; NP_214959.1; NC_000962.3.
DR RefSeq; WP_003402246.1; NZ_NVQJ01000002.1.
DR PDB; 4NQW; X-ray; 2.40 A; A=1-187.
DR PDBsum; 4NQW; -.
DR AlphaFoldDB; P9WGH7; -.
DR SMR; P9WGH7; -.
DR STRING; 83332.Rv0445c; -.
DR PaxDb; P9WGH7; -.
DR DNASU; 886334; -.
DR GeneID; 886334; -.
DR KEGG; mtu:Rv0445c; -.
DR TubercuList; Rv0445c; -.
DR eggNOG; COG1595; Bacteria.
DR OMA; KGRFFTW; -.
DR PhylomeDB; P9WGH7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR039425; RNA_pol_sigma-70-like.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR43133; PTHR43133; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR SUPFAM; SSF88659; SSF88659; 1.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..187
FT /note="ECF RNA polymerase sigma factor SigK"
FT /id="PRO_0000313845"
FT DNA_BIND 155..174
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 30..96
FT /note="Sigma-70 factor domain-2"
FT REGION 133..182
FT /note="Sigma-70 factor domain-4"
FT MOTIF 53..56
FT /note="Interaction with polymerase core subunit RpoC"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 25..45
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4NQW"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 76..94
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:4NQW"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 166..184
FT /evidence="ECO:0007829|PDB:4NQW"
SQ SEQUENCE 187 AA; 21035 MW; 2156CEB813620F02 CRC64;
MTGPPRLSSD LDALLRRVAG HDQAAFAEFY DHTKSRVYGL VMRVLRDTGY SEETTQEIYL
EVWRNASEFD SAKGSALAWL LTMAHRRAVD RVRCEQAGNQ REVRYGAANV DPASDVVADL
AIAGDERRRV TECLKALTDT QRQCIELAYY GGLTYVEVSR RLAANLSTIK SRMRDALRSL
RNCLDVS
