ID A0A0Q5V0J9_9CAUL Unreviewed; 499 AA.
AC A0A0Q5V0J9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN ORFNames=ASG17_03485 {ECO:0000313|EMBL:KQS55168.1};
OS Brevundimonas sp. Leaf363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS55168.1, ECO:0000313|Proteomes:UP000051182};
RN [1] {ECO:0000313|EMBL:KQS55168.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55168.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS55168.1, ECO:0000313|Proteomes:UP000051182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55168.1,
RC ECO:0000313|Proteomes:UP000051182};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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. {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:KQS55168.1}.
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DR EMBL; LMPZ01000002; KQS55168.1; -; Genomic_DNA.
DR RefSeq; WP_056099247.1; NZ_LMPZ01000002.1.
DR AlphaFoldDB; A0A0Q5V0J9; -.
DR STRING; 1736353.ASG17_03485; -.
DR OrthoDB; 9814402at2; -.
DR Proteomes; UP000051182; 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 Reference proteome {ECO:0000313|Proteomes:UP000051182};
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 135..319
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 334..494
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 43..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 54126 MW; D0749272590BAB77 CRC64;
MLGQRLEVRQ GQGLVVTPQL QQAIKLLQLS NQELDAFVEQ ELERNPLLQR DEPEGETGDA
PAATEAADRA EMSFDDGRAQ DGGDAVDARS DDVHGEASPG ERASDRAAED SQPGLSDWSR
VGAGGSAPEG DYERPDEHEA TLWEHLQAQA SQAAFSAPDQ AIALTLIDAV DEGGYLRIEL
AEVADRLGCA LERVEAVLAV CHGFEPTGVM ARTVPECLKL QLIERNRFDP AMAALLDNLE
LLARRDLIGL KKVCGVDGED LTDMIAELRG LTPRPGAGFG GEPAQTVIPD VHVRPDPAGG
WRVELNADTL PRLLIDKRYH GVVQAGARTE TEKTFVADCA AQASWLVKSL DQRAKTILKV
GSEIVRQQDA FLAFGVEFLR PLNLKTVADA IGMHESTVSR VTSNKYVSTP RGVFELKFFF
TAAIQSVDGA STHSAEAVRH RIKSMIDAEG SDGDVLSDDR IVEILKEAGI DIARRTVAKY
REALRIPSSV ARKRMLKTA
//
