GenomeNet

Database: UniProt
Entry: A0A178A3N5_9BACI
LinkDB: A0A178A3N5_9BACI
Original site: A0A178A3N5_9BACI 
ID   A0A178A3N5_9BACI        Unreviewed;       376 AA.
AC   A0A178A3N5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   18-JUN-2025, entry version 34.
DE   RecName: Full=RNA polymerase sigma factor SigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   Name=sigA {ECO:0000256|HAMAP-Rule:MF_00963};
GN   ORFNames=ABB05_03825 {ECO:0000313|EMBL:OAK74704.1};
OS   Lederbergia galactosidilytica.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Lederbergia.
OX   NCBI_TaxID=217031 {ECO:0000313|EMBL:OAK74704.1, ECO:0000313|Proteomes:UP000077881};
RN   [1] {ECO:0000313|EMBL:OAK74704.1, ECO:0000313|Proteomes:UP000077881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-74 {ECO:0000313|EMBL:OAK74704.1,
RC   ECO:0000313|Proteomes:UP000077881};
RA   Zheng Z., Sun M.;
RT   "Comparison of genome.";
RL   Submitted (MAY-2015) 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. This sigma factor is the primary sigma factor during
CC       exponential growth. {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBUNIT: Interacts transiently with the RNA polymerase catalytic core.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00963}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAK74704.1}.
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; LDJR01000021; OAK74704.1; -; Genomic_DNA.
DR   RefSeq; WP_057983083.1; NZ_JAGGKH010000006.1.
DR   AlphaFoldDB; A0A178A3N5; -.
DR   STRING; 217031.ABB05_03825; -.
DR   PATRIC; fig|217031.6.peg.832; -.
DR   OrthoDB; 9809557at2; -.
DR   Proteomes; UP000077881; Unassembled WGS sequence.
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   CDD; cd06171; Sigma70_r4; 1.
DR   FunFam; 1.10.10.10:FF:000002; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.10.10:FF:000004; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.601.10:FF:000001; RNA polymerase sigma factor SigA; 1.
DR   FunFam; 1.10.601.10:FF:000003; RNA polymerase sigma factor SigA; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 2.
DR   Gene3D; 1.10.220.120; Sigma-70 factor, region 1.1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
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; IPR050239; Sigma-70_RNA_pol_init_factors.
DR   InterPro; IPR028630; Sigma70_RpoD.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; NF006666; PRK09210.1; 1.
DR   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF60; RNA POLYMERASE SIGMA FACTOR RPOD; 1.
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; SSF88946; Sigma2 domain of RNA polymerase sigma factors; 1.
DR   SUPFAM; SSF88659; Sigma3 and sigma4 domains of RNA polymerase sigma factors; 2.
DR   PROSITE; PS00715; SIGMA70_1; 1.
DR   PROSITE; PS00716; SIGMA70_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00963};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00963}; Reference proteome {ECO:0000313|Proteomes:UP000077881};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00963};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00963}.
FT   DOMAIN          167..180
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          336..362
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        337..356
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          143..213
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          222..298
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          311..364
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   COILED          298..325
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           167..170
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
SQ   SEQUENCE   376 AA;  43263 MW;  6B043F257D659FE2 CRC64;
     MAEKSARSNE TVNELTVDQA KEQLIEQGKK VGTLTYEKIG EKLGHFDLDS DQLDEFYEHL
     TDQGVELVED SDEDEDPNVT DIQKEDEEEF DLNDLSVPPG VKINDPVRMY LKEIGRVDLL
     SAEEEVELAK RIEQGDEEAK KRLAEANLRL VVSIAKRYVG RGMLFLDLIQ EGNMGLIKAV
     EKFDYDKGFK FSTYATWWIR QAITRAIADQ ARTIRIPVHM VETINKLIRV QRQLLQDLGR
     EPTPEEIAEE MDMTPDKVRE ILKIAQEPVS LETPIGEEDD SHLGDFIEDQ EATSPSEHAA
     YELLKEQLED VLDTLTDREE NVLRLRFGLD DGRTRTLEEV GKVFGVTRER IRQIEAKALR
     KLRHPSRSKR LKDFLE
//
DBGET integrated database retrieval system