ID A0A1I2CQ01_9BACT Unreviewed; 495 AA.
AC A0A1I2CQ01;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=RNA polymerase, sigma 54 subunit, RpoN/SigL {ECO:0000313|EMBL:SFE70427.1};
GN ORFNames=SAMN05518672_109128 {ECO:0000313|EMBL:SFE70427.1};
OS Chitinophaga sp. CF118.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFE70427.1, ECO:0000313|Proteomes:UP000199596};
RN [1] {ECO:0000313|EMBL:SFE70427.1, ECO:0000313|Proteomes:UP000199596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF118 {ECO:0000313|EMBL:SFE70427.1,
RC ECO:0000313|Proteomes:UP000199596};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sigma-54 factor family.
CC {ECO:0000256|ARBA:ARBA00008798}.
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DR EMBL; FOMK01000009; SFE70427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2CQ01; -.
DR STRING; 1884367.SAMN05518672_109128; -.
DR OrthoDB; 9814402at2; -.
DR Proteomes; UP000199596; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; 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; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.10.1330; RNA polymerase sigma-54 factor, core-binding domain; 1.
DR InterPro; IPR000394; RNA_pol_sigma_54.
DR InterPro; IPR007046; RNA_pol_sigma_54_core-bd.
DR InterPro; IPR007634; RNA_pol_sigma_54_DNA-bd.
DR InterPro; IPR038709; RpoN_core-bd_sf.
DR NCBIfam; TIGR02395; rpoN_sigma; 1.
DR PANTHER; PTHR32248; RNA POLYMERASE SIGMA-54 FACTOR; 1.
DR PANTHER; PTHR32248:SF4; RNA POLYMERASE SIGMA-54 FACTOR; 1.
DR Pfam; PF00309; Sigma54_AID; 1.
DR Pfam; PF04963; Sigma54_CBD; 1.
DR Pfam; PF04552; Sigma54_DBD; 1.
DR PIRSF; PIRSF000774; RpoN; 1.
DR PRINTS; PR00045; SIGMA54FCT.
DR PROSITE; PS00718; SIGMA54_2; 1.
DR PROSITE; PS50044; SIGMA54_3; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Sigma factor {ECO:0000256|ARBA:ARBA00023082};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 122..313
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 336..493
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 38..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 57185 MW; FC669D6897E4333F CRC64;
MLKQTQQQKL LQKLSPQQIQ LMKLLQVPTA VLEERIKEEL EENPALEYGE EAQEDEFKET
QEEFTTPEEE DEFEPDGSEN EYDNIDISEY VSEGDDDIAD YRLRDDNYPD PDENKTIPVR
VETSFHEHLL AQLGMLALDE RQTSIAEQII GSIDDDGYLR REISAIVDDL SFSQNVSTDE
EEIKDLIKKI QEFDPPGICA TDLKECLLLQ LKRKIQDDPG VMGAYQILEN YFDEFTKKHY
EKIQKGLNMS DEALKEAIGQ IIRLTPKPGG NYATLNKAES YVIPDFFILN NNGKLELSLN
SKNAPDLRIS EGYRDMLKDY DRGDKKDKRQ KEAVLFIKQK IDAAKWFIDA IKQRQHTLLS
TMESIMGYQR EFFLTGDETT MRPMILKDIA DITQLDISTV SRVANSKYVQ TEFGTFKLKF
FFSESLSTDS GEEVSTREVK KILSDLIEGE NKRKPLSDEN LTKMLQDKGY NIARRTVAKY
REQLNIPVAR LRKEL
//