ID C3XAZ7_OXAFO Unreviewed; 490 AA.
AC C3XAZ7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN Name=rpoN {ECO:0000313|EMBL:EEO30373.1};
GN ORFNames=OFBG_01401 {ECO:0000313|EMBL:EEO30373.1};
OS Oxalobacter formigenes OXCC13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO30373.1, ECO:0000313|Proteomes:UP000005089};
RN [1] {ECO:0000313|EMBL:EEO30373.1, ECO:0000313|Proteomes:UP000005089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO30373.1,
RC ECO:0000313|Proteomes:UP000005089};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allison M.J., Lander E., Nusbaum C., Galagan J.,
RA Birren B.;
RT "The Genome Sequence of Oxalobacter formigenes OXCC13.";
RL Submitted (FEB-2009) 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; GG658170; EEO30373.1; -; Genomic_DNA.
DR RefSeq; WP_005881476.1; NZ_GG658170.1.
DR AlphaFoldDB; C3XAZ7; -.
DR STRING; 847.BRW83_0707; -.
DR GeneID; 77134609; -.
DR eggNOG; COG1508; Bacteria.
DR HOGENOM; CLU_020569_0_1_4; -.
DR OrthoDB; 9814402at2; -.
DR Proteomes; UP000005089; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000005089};
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 128..320
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 333..489
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 55..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..50
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 55446 MW; 93214699EA9ED3D8 CRC64;
MKQKLQTSFS QHLALTPQLQ QSIRLLQLSS QELNQELEQA LQENPLLERV DDPLATSTRL
SGDGSVISTT KQPETASHTD SGDFSGERTG DVSSNEEHTS DSERMDSLWN VPVPSERQPD
DERSKPQIEA PPESLREHLI SQMRLSVISQ RQRALVELII DALDANGFLQ ESLPEMLEWL
PQELDISLKE LEEALSCVQD FEPAGVGART SAECLAIQIR LLPRIPYVVR KRAMNIVENH
LELFARHDFV RLKKVLECDD EDLKEAQEVI HRCNPHPGAI YATDTAETVI PEIIVSKKEN
CWVAELNPDA MPKIRVNQLY ANILRESGSK AALSVQLREA KWLIRNINQR YETILKTSQA
IVERQQNFFS FGATSMRPLV LREIADTLGL HESTISRVSN QKFMRTPHGI LELKYFFGSS
VATETGGEAS STAIREKIRQ LIETEDKKKP LSDNRIAQLL ERQGLVVARR TVAKYRDILK
IPPASLRKKL
//
