SIGK_MYCVP
ID SIGK_MYCVP Reviewed; 196 AA.
AC A1TEV0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Mvan_4927;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM15700.1; -; Genomic_DNA.
DR AlphaFoldDB; A1TEV0; -.
DR SMR; A1TEV0; -.
DR STRING; 350058.Mvan_4927; -.
DR EnsemblBacteria; ABM15700; ABM15700; Mvan_4927.
DR KEGG; mva:Mvan_4927; -.
DR eggNOG; COG1595; Bacteria.
DR HOGENOM; CLU_047691_9_3_11; -.
DR OMA; KGRFFTW; -.
DR Proteomes; UP000009159; Chromosome.
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 3: Inferred from homology;
KW DNA-binding; Reference proteome; Sigma factor; Transcription;
KW Transcription regulation.
FT CHAIN 1..196
FT /note="ECF RNA polymerase sigma factor SigK"
FT /id="PRO_0000313847"
FT DNA_BIND 164..183
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 39..105
FT /note="Sigma-70 factor domain-2"
FT REGION 142..191
FT /note="Sigma-70 factor domain-4"
FT MOTIF 62..65
FT /note="Polymerase core binding"
SQ SEQUENCE 196 AA; 21632 MW; A90A58C5E977B1D3 CRC64;
MTASVLVGAA ARLPLVTAEL DALLRQVAQR DAEAFAAFYD QTRARVYGLI TRVLRDPGYS
EETTQDVYLQ VWRNAAGYDP SVGSALSWLL TLAHRRAVDR VRSEQAASTR ESRYGAISVD
PPSDHVADDV LLDDERRRVA GCLDSLTDVQ RECIQLAYYD GLTYAQVADR LAANLATIKS
RMRDGIRALR KCLGVA
