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Database: UniProt
Entry: A0A0K1K0M8_9BURK
LinkDB: A0A0K1K0M8_9BURK
Original site: A0A0K1K0M8_9BURK 
ID   A0A0K1K0M8_9BURK        Unreviewed;       491 AA.
AC   A0A0K1K0M8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=ACZ75_16255 {ECO:0000313|EMBL:AKU22788.1};
OS   Massilia sp. NR 4-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU22788.1, ECO:0000313|Proteomes:UP000056897};
RN   [1] {ECO:0000313|EMBL:AKU22788.1, ECO:0000313|Proteomes:UP000056897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU22788.1,
RC   ECO:0000313|Proteomes:UP000056897};
RA   Sul W.J.;
RT   "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT   national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL   Submitted (JUN-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; CP012201; AKU22788.1; -; Genomic_DNA.
DR   RefSeq; WP_050409695.1; NZ_CP012201.1.
DR   AlphaFoldDB; A0A0K1K0M8; -.
DR   STRING; 1678028.ACZ75_16255; -.
DR   KEGG; mnr:ACZ75_16255; -.
DR   PATRIC; fig|1678028.3.peg.3299; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000056897; 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   Reference proteome {ECO:0000313|Proteomes:UP000056897};
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          130..321
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          334..489
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          67..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  54436 MW;  3A92B8BAE0BBA1CE CRC64;
     MKQSLQLRTS QHLALTPQLQ QSIRLLQLST LELHQELEQL LTDNPLLERL DDPLDRSVRL
     LADGAISQTS TPGEAPPDNA APADAPAPAA EAEPAYEGGE GESVAEADGD WGDTGRGKAP
     EDDDARPQLE AHHCSLREHL LEQMRVTLQE PRDRALMELI VDALDDNGYL DESLEEIHAR
     LPLELDVELE ELQTSLTLLQ SFDPAGVGAR SAAECLALQI RRLPGVPLVT RRMALCIVEK
     HLAWFAQREF TKLKKALDCD DEDLREAQTV IRQCNPHPGA AFAADVSDYV VPDVVVKKGR
     NGWIVMLNND VMPRLRVNSL YASLLRQGKG ETQMSAQLQE AKWLIKNMRQ RFDTILRVAQ
     AIVERQKNFF SHGAVAMRPL VLREIADTLG LHESTISRVT TQKYMLTPHG MFELKYFFGS
     HVATEAGGEA SSTAIRALIV QLTGAEDPKN PLSDSKIADM LGEQGMVIAR RTVAKYREAL
     KIPPVSLRKS L
//
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