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Database: UniProt
Entry: A0A249LHA2_9ACTN
LinkDB: A0A249LHA2_9ACTN
Original site: A0A249LHA2_9ACTN 
ID   A0A249LHA2_9ACTN        Unreviewed;       494 AA.
AC   A0A249LHA2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=PHILAsVB114_04385 {ECO:0000313|EMBL:ASY28377.1};
OS   Candidatus Planktophila limnetica.
OC   Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC   Candidatus Nanopelagicaceae; Planktophila.
OX   NCBI_TaxID=573600 {ECO:0000313|EMBL:ASY28377.1, ECO:0000313|Proteomes:UP000217221};
RN   [1] {ECO:0000313|EMBL:ASY28377.1, ECO:0000313|Proteomes:UP000217221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-VB-114 {ECO:0000313|EMBL:ASY28377.1};
RA   Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT   "High microdiversification within the ubiquitous acI lineage of
RT   Actinobacteria.";
RL   Submitted (JUL-2016) 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}.
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DR   EMBL; CP016782; ASY28377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A249LHA2; -.
DR   KEGG; plim:PHILAsVB114_04385; -.
DR   Proteomes; UP000217221; 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   CDD; cd06171; Sigma70_r4; 1.
DR   Gene3D; 1.20.120.1810; -; 1.
DR   Gene3D; 1.10.601.10; RNA Polymerase Primary Sigma Factor; 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; 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   NCBIfam; TIGR02393; RpoD_Cterm; 1.
DR   NCBIfam; TIGR02937; sigma70-ECF; 1.
DR   PANTHER; PTHR30603; RNA POLYMERASE SIGMA FACTOR RPO; 1.
DR   PANTHER; PTHR30603:SF47; RNA POLYMERASE SIGMA FACTOR SIGF, CHLOROPLASTIC; 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   Cytoplasm {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:UP000217221};
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          285..298
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00715"
FT   DOMAIN          454..480
FT                   /note="RNA polymerase sigma-70"
FT                   /evidence="ECO:0000259|PROSITE:PS00716"
FT   DNA_BIND        455..474
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          261..331
FT                   /note="Sigma-70 factor domain-2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          340..416
FT                   /note="Sigma-70 factor domain-3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   REGION          429..482
FT                   /note="Sigma-70 factor domain-4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
FT   MOTIF           285..288
FT                   /note="Interaction with polymerase core subunit RpoC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00963"
SQ   SEQUENCE   494 AA;  55139 MW;  B2D9467774C0B1B0 CRC64;
     MVPKKIELKK DLTAKDVQAI VDAKTIATRQ KEVLAELESR GVTSINRIPK KSDKDLVDEA
     RALAVTVPVA TEKLRKAGLG SPFRMLKKVE LELIAPPAPK VVAPKIDAKT GKPVVVKIDG
     QEVEVEEVDL EDVESLIAEA VEIIDSEAED KGNQPRVVDL KAEDATGNEE NAFTLKASEE
     DDAPAQTVMT AGATADPVKD YLKQIGRVAL LNAELEVELA TRVEAGLFAE YKLFTEKKLD
     KKLKRELEFI VEDGKRAKNH LLEANLRLVV SLAKRYTGRG MLFLDLIQEG NLGLIRAVEK
     FDYTKGYKFS TYATWWIRQA ITRAMADQAR TIRIPVHMVE VINKLARVQR QMLQDLGREP
     TPEELARELD MTPEKVVEVQ KYGREPISLH TPLGEEGDSE FGDLIEDSEA VVPADAVSFT
     LLQEQLHSVL DTLSEREAGV VAMRFGLTDG QPKTLDEIGK VYGVTRERIR QIESKTMSKL
     RHPSRSQVLR DYLD
//
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