ID SIGK_MYCSJ Reviewed; 193 AA.
AC A3Q5U0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=Mjls_4752;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
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; CP000580; ABO00518.1; -; Genomic_DNA.
DR AlphaFoldDB; A3Q5U0; -.
DR SMR; A3Q5U0; -.
DR KEGG; mjl:Mjls_4752; -.
DR HOGENOM; CLU_047691_9_3_11; -.
DR BioCyc; MSP164757:G1G8C-4797-MONOMER; -.
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 CDD; cd06171; Sigma70_r4; 1.
DR Gene3D; 1.10.1740.10; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 NCBIfam; TIGR02937; sigma70-ECF; 1.
DR PANTHER; PTHR43133:SF70; ECF RNA POLYMERASE SIGMA FACTOR SIGK; 1.
DR PANTHER; PTHR43133; RNA POLYMERASE ECF-TYPE SIGMA FACTO; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR SUPFAM; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1.
DR SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 1.
PE 3: Inferred from homology;
KW DNA-binding; Sigma factor; Transcription; Transcription regulation.
FT CHAIN 1..193
FT /note="ECF RNA polymerase sigma factor SigK"
FT /id="PRO_0000313841"
FT DNA_BIND 161..180
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 35..101
FT /note="Sigma-70 factor domain-2"
FT REGION 140..187
FT /note="Sigma-70 factor domain-4"
FT MOTIF 59..62
FT /note="Polymerase core binding"
SQ SEQUENCE 193 AA; 21716 MW; 44A5983BB3B16F96 CRC64;
MTALTQPVRL PFVTTDLDVL LRQVAERDVD AFAALYDRTR SRVYGMVTRV LRDPGYSEET
TQDIYLQVWR SAGSYDPKAG SPMAWLLTLA HRRAVDRVRS EEAASQRESR YGAASVDPPV
DHVADSVILL DERRRVVDCM GSLSDLQREA IQLAYYEGLT YVQVSERLSA NLATIKSRMR
DGIRGLKNCL GMS
//
