ID K7A418_9ALTE Unreviewed; 497 AA.
AC K7A418;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN Name=rpoN {ECO:0000313|EMBL:GAC35623.1};
GN ORFNames=GPLA_4749 {ECO:0000313|EMBL:GAC35623.1};
OS Paraglaciecola polaris LMG 21857.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129793 {ECO:0000313|EMBL:GAC35623.1, ECO:0000313|Proteomes:UP000006322};
RN [1] {ECO:0000313|EMBL:GAC35623.1, ECO:0000313|Proteomes:UP000006322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21857 {ECO:0000313|EMBL:GAC35623.1,
RC ECO:0000313|Proteomes:UP000006322};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC35623.1}.
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DR EMBL; BAER01000145; GAC35623.1; -; Genomic_DNA.
DR RefSeq; WP_007107383.1; NZ_BAER01000145.1.
DR AlphaFoldDB; K7A418; -.
DR STRING; 1129793.GPLA_4749; -.
DR OrthoDB; 9814402at2; -.
DR Proteomes; UP000006322; 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 136..323
FT /note="RNA polymerase sigma factor 54 core-binding"
FT /evidence="ECO:0000259|Pfam:PF04963"
FT DOMAIN 337..494
FT /note="RNA polymerase sigma factor 54 DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04552"
FT REGION 50..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 55664 MW; E0E57A82CCA5C7FA CRC64;
MKPSLQLKFS QSLTMTPQLQ QAIRLLQLST LDLQLEIQEA LDSNPLLEIE EPTDQESGDS
ALNDNSLDPA SKESNEVVDT SSDNIDASEA LEKNDIPEDL PMDTTWDEYI SASSAPASSI
SSGAAGDDEQ IFQGETTDNI QDHLLWQMRL THFSETDIAI ATAIIDSIDE SGYLTMSAED
VLASMDDEEI ELDEVECVLK RIQMFDPIGS GSRTPQECLL VQLRQFAPDT PWLEEAKTLI
SEYADLLSSK DYRTLMRKSR LKEDDLREVM RLLKTLNPRP GSALIKGEPE YVIPDVSVSK
KNGRWTVELN PDSLPKLNVN QQYAAMSRGA KNTSDSQFIR SHMQEAKWFI KSVESRNDTL
LKVSNCIVQQ QMGFFEHGPE MMKPMVLNDV AEMVDMHEST ISRVTTQKYM HTPRGIFELK
YFFSSHVATE TGGECSSTAI RALIKKLVAA EKPSKPLSDS KIAQLLADQG IMVARRTIAK
YRESLMIPPS NQRKSLL
//