ID A0A127PYS0_9BURK Unreviewed; 493 AA.
AC A0A127PYS0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN Name=rpoN {ECO:0000313|EMBL:AMP02937.1};
GN ORFNames=CPter291_0461 {ECO:0000313|EMBL:AMP12747.1}, CPter91_0542
GN {ECO:0000313|EMBL:AMP02937.1};
OS Collimonas pratensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP02937.1, ECO:0000313|Proteomes:UP000074561};
RN [1] {ECO:0000313|Proteomes:UP000074561, ECO:0000313|Proteomes:UP000074914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter291 {ECO:0000313|EMBL:AMP12747.1,
RC ECO:0000313|Proteomes:UP000074914}, and Ter91
RC {ECO:0000313|EMBL:AMP02937.1, ECO:0000313|Proteomes:UP000074561};
RA Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT "Exploring the genomic traits of fungus-feeding bacterial genus
RT Collimonas.";
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}.
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DR EMBL; CP013234; AMP02937.1; -; Genomic_DNA.
DR EMBL; CP013236; AMP12747.1; -; Genomic_DNA.
DR RefSeq; WP_061936483.1; NZ_CP013236.1.
DR AlphaFoldDB; A0A127PYS0; -.
DR STRING; 279113.CPter91_0542; -.
DR KEGG; cpra:CPter91_0542; -.
DR PATRIC; fig|279113.10.peg.460; -.
DR OrthoDB; 9814402at2; -.
DR Proteomes; UP000074561; Chromosome.
DR Proteomes; UP000074914; Chromosome.
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 131..323
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 336..491
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 69..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 55007 MW; 445A14E0C29416BE CRC64;
MKQSLQLRTS QHLALTPQLQ QSIRLLQLST LELHQELEQI LSDNPMLERV DDPLDNSVRL
LADGAISGTA STMEAPTGDS EVSSSPTESE ASLETPAAAD SSSDNSDSDW SFDDISRSAK
SSDDEDARPQ LEAHESTLRE HLLQQMREAM RDLRDRALVE LVIDALDDNG YLEESLEEIL
ERLPPELEIA LEELSMALKM VQSFDPAGVG ARNAPECLGL QIKRFVKVPF VTRRLALAIV
QEHLVLFAQR DFNKIKKALD CDDEDLREAQ TVIKQCNPHP GAPFAGNASD YVVPDVIVRR
SKQGWQVMLN NDVMPRLRVN VLYANILKQS KGDGALTSQL QEAKWLIKNM RQRFDTILRV
AQAIVERQRN FFSHGAVAMR PLVLREIADT LGLHESTISR VTTQKYMLTP HGMFELKYFF
GSHVATEAGG EASSTAIRAL IKQLIGAEDS RNPFSDSKIA DMLAEQGMVV ARRTVAKYRE
ALKIPSVNLR KAL
//
