ID   A0A2A5GFG1_9GAMM        Unreviewed;       492 AA.
AC   A0A2A5GFG1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=COA46_09100 {ECO:0000313|EMBL:PCJ91096.1};
OS   Porticoccaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae.
OX   NCBI_TaxID=2026782 {ECO:0000313|EMBL:PCJ91096.1, ECO:0000313|Proteomes:UP000230152};
RN   [1] {ECO:0000313|Proteomes:UP000230152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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. {ECO:0000256|PIRNR:PIRNR000774}.
CC   -!- SIMILARITY: Belongs to the sigma-54 factor family.
CC       {ECO:0000256|ARBA:ARBA00008798, ECO:0000256|PIRNR:PIRNR000774}.
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:PCJ91096.1}.
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DR   EMBL; NVXH01000009; PCJ91096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5GFG1; -.
DR   Proteomes; UP000230152; 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; PS00717; SIGMA54_1; 1.
DR   PROSITE; PS00718; SIGMA54_2; 1.
DR   PROSITE; PS50044; SIGMA54_3; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000774};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Sigma factor {ECO:0000256|ARBA:ARBA00023082,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PIRNR:PIRNR000774};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000774}.
FT   DOMAIN          123..315
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          329..487
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          53..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  55298 MW;  34E9F3A02D5BF855 CRC64;
     MKISLQLKIG QQLTMTPQLQ QAIRLLQLSS LDLHQEIQQN LYDNPLLELA EESEDLPENT
     SENSAHNAET KPLEEAPDSA TQDLNGDDWG TKIPQDLPVD ANWDDIYQPT TSLKNTSSEP
     LDFENVHHVT ESLRDHLLWQ LNLTTVSTTD HLIAENIIDS INNDGMLTTS AEDIWASLSD
     EIELDEVVAV LHLIQQFDPP GVGATTLSEC LLIQLKQFST ETPLLEEAKK LVSNHLDLVG
     MRDYRKLEKL TGYTQATVEA VTALIQTLSP HPGESITNDD VEYIVPDARV TKVNDHWRVS
     LNHDITPKLS INQQYAKLIR RADSSEDNTF LKTHLQEAKW FLRSIESRND TLLRVSSCII
     ELQQQFLEQG AEAMRPMVLA NIAEQLDLHE STISRVTTKK YIDTPQGVFE LKYFFSSHVA
     TASGGECSST AIRAILKKMI NAESPAKPLS DNKLTTLLQD MGIQVARRTV AKYREGMGIP
     SSSERKRFKH TI
//