SIGA_STAA8
ID SIGA_STAA8 Reviewed; 368 AA.
AC P0A0J0; P26766; Q2FY12;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=RNA polymerase sigma factor SigA {ECO:0000255|HAMAP-Rule:MF_00963};
GN Name=sigA {ECO:0000255|HAMAP-Rule:MF_00963}; Synonyms=plaC, rpoD;
GN OrderedLocusNames=SAOUHSC_01662;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1923759; DOI=10.1093/nar/19.18.4921;
RA Basheer R., Iordanescu S.;
RT "The Staphylococcus aureus chromosomal gene plaC, identified by mutations
RT amplifying plasmid pT181, encodes a sigma factor.";
RL Nucleic Acids Res. 19:4921-4924(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 297-368 IN COMPLEX WITH PHAGE
RP PROTEIN GP67, FUNCTION, AND SUBUNIT.
RX PubMed=23178120; DOI=10.1016/j.cell.2012.10.034;
RA Osmundson J., Montero-Diez C., Westblade L.F., Hochschild A., Darst S.A.;
RT "Promoter-specific transcription inhibition in Staphylococcus aureus by a
RT phage protein.";
RL Cell 151:1005-1016(2012).
CC -!- FUNCTION: Sigma factors are initiation factors that promote the
CC attachment of RNA polymerase to specific initiation sites and are then
CC released. This sigma factor is the primary sigma factor during
CC exponential growth. {ECO:0000255|HAMAP-Rule:MF_00963,
CC ECO:0000269|PubMed:23178120}.
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 (By similarity). Interacts (via sigma-70 factor domain 4)
CC with the phage G1 protein gp67; this inhibits rRNA synthesis.
CC Interaction with phage G1 protein gp67 does not inhibit transcription
CC in general, but selectively inhibits transcription from promoters that
CC require interaction of the RNA polymerase alpha subunit with DNA
CC sequences upstream of the -35 promoter element. {ECO:0000255|HAMAP-
CC Rule:MF_00963, ECO:0000269|PubMed:23178120}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00963}.
CC -!- DOMAIN: Contains 4 domains, connected by flexible linkers. In the
CC active conformation, the domains are in an extended conformation, each
CC making extensive interactions with the RNA polymerase catalytic core
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: In the autoinhibited state, sigma-70 factor domain-1 packs
CC closely together with sigma-70 factor domains-2 and -4, contrary to the
CC extended conformation that is seen when the protein is part of the RNA
CC polymerase holoenzyme. {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 -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00963}.
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DR EMBL; M63177; AAB59090.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30737.1; -; Genomic_DNA.
DR PIR; S34442; S34442.
DR RefSeq; WP_001283055.1; NZ_LS483365.1.
DR RefSeq; YP_500173.1; NC_007795.1.
DR PDB; 4G6D; X-ray; 2.00 A; A=297-368.
DR PDB; 4G8X; X-ray; 3.00 A; A/C=297-357.
DR PDB; 4G94; X-ray; 2.00 A; A=297-357.
DR PDBsum; 4G6D; -.
DR PDBsum; 4G8X; -.
DR PDBsum; 4G94; -.
DR AlphaFoldDB; P0A0J0; -.
DR SMR; P0A0J0; -.
DR STRING; 1280.SAXN108_1583; -.
DR EnsemblBacteria; ABD30737; ABD30737; SAOUHSC_01662.
DR GeneID; 3920074; -.
DR KEGG; sao:SAOUHSC_01662; -.
DR PATRIC; fig|93061.5.peg.1512; -.
DR eggNOG; COG0568; Bacteria.
DR HOGENOM; CLU_014793_3_3_9; -.
DR OMA; YQRWLAE; -.
DR PRO; PR:P0A0J0; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 1.10.220.120; -; 1.
DR HAMAP; MF_00963; Sigma70_RpoD_SigA; 1.
DR InterPro; IPR014284; RNA_pol_sigma-70_dom.
DR InterPro; IPR000943; RNA_pol_sigma70.
DR InterPro; IPR009042; RNA_pol_sigma70_r1_2.
DR InterPro; IPR007627; RNA_pol_sigma70_r2.
DR InterPro; IPR007624; RNA_pol_sigma70_r3.
DR InterPro; IPR007630; RNA_pol_sigma70_r4.
DR InterPro; IPR007127; RNA_pol_sigma_70_r1_1.
DR InterPro; IPR042189; RNA_pol_sigma_70_r1_1_sf.
DR InterPro; IPR013325; RNA_pol_sigma_r2.
DR InterPro; IPR013324; RNA_pol_sigma_r3/r4-like.
DR InterPro; IPR012760; RNA_pol_sigma_RpoD_C.
DR InterPro; IPR028630; Sigma70_RpoD.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF03979; Sigma70_r1_1; 1.
DR Pfam; PF00140; Sigma70_r1_2; 1.
DR Pfam; PF04542; Sigma70_r2; 1.
DR Pfam; PF04539; Sigma70_r3; 1.
DR Pfam; PF04545; Sigma70_r4; 1.
DR PRINTS; PR00046; SIGMA70FCT.
DR SUPFAM; SSF88659; SSF88659; 2.
DR SUPFAM; SSF88946; SSF88946; 1.
DR TIGRFAMs; TIGR02393; RpoD_Cterm; 1.
DR TIGRFAMs; TIGR02937; sigma70-ECF; 1.
DR PROSITE; PS00715; SIGMA70_1; 1.
DR PROSITE; PS00716; SIGMA70_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Reference proteome; Sigma factor;
KW Transcription; Transcription regulation.
FT CHAIN 1..368
FT /note="RNA polymerase sigma factor SigA"
FT /id="PRO_0000093916"
FT DNA_BIND 329..348
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00963"
FT REGION 16..90
FT /note="Sigma-70 factor domain-1"
FT REGION 69..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..205
FT /note="Sigma-70 factor domain-2"
FT REGION 214..291
FT /note="Sigma-70 factor domain-3"
FT REGION 303..356
FT /note="Sigma-70 factor domain-4"
FT MOTIF 159..162
FT /note="Interaction with polymerase core subunit RpoC"
FT VARIANT 209
FT /note="P -> S (in plaC1 mutation; results in a narrower
FT specificity for promoters)"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:4G6D"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:4G6D"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:4G6D"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:4G6D"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:4G6D"
SQ SEQUENCE 368 AA; 42171 MW; AB029CA4F5A93A55 CRC64;
MSDNTVKIKK QTIDPTLTLE DVKKQLIEKG KKEGHLSHEE IAEKLQNFDI DSDQMDDFFD
QLNDNDISLV NEKDSSDTDE KLNPSDLSAP PGVKINDPVR MYLKEIGRVN LLSAQEEIEL
AKRIEQGDEV AKSRLAEANL RLVVSIAKRY VGRGMLFLDL IQEGNMGLIK AVEKFDFNKG
FKFSTYATWW IRQAITRAIA DQARTIRIPV HMVETINKLI RVQRQLLQDL GRDPAPEEIG
EEMDLPAEKV REILKIAQEP VSLETPIGEE DDSHLGDFIE DQEAQSPSDH AAYELLKEQL
EDVLDTLTDR EENVLRLRFG LDDGRTRTLE EVGKVFGVTR ERIRQIEAKA LRKLRHPSRS
KRLKDFMD
