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Database: UniProt
Entry: A4CF32_9GAMM
LinkDB: A4CF32_9GAMM
Original site: A4CF32_9GAMM 
ID   A4CF32_9GAMM            Unreviewed;       495 AA.
AC   A4CF32;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   13-SEP-2023, entry version 66.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=PTD2_17247 {ECO:0000313|EMBL:EAR26707.1};
OS   Pseudoalteromonas tunicata D2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR26707.1, ECO:0000313|Proteomes:UP000006201};
RN   [1] {ECO:0000313|EMBL:EAR26707.1, ECO:0000313|Proteomes:UP000006201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D2 {ECO:0000313|EMBL:EAR26707.1,
RC   ECO:0000313|Proteomes:UP000006201};
RA   Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA   Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA   Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR26707.1}.
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DR   EMBL; AAOH01000010; EAR26707.1; -; Genomic_DNA.
DR   RefSeq; WP_009840691.1; NZ_CH959302.1.
DR   AlphaFoldDB; A4CF32; -.
DR   STRING; 87626.PTD2_17247; -.
DR   eggNOG; COG1508; Bacteria.
DR   HOGENOM; CLU_020569_0_1_6; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000006201; 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          129..321
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          335..492
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          54..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  55952 MW;  699EB206A28B11F1 CRC64;
     MRQSLQLRLG QQLTMTPQLQ QAIRLLQLST LDLQQEIQEA LDSNPLLELE ETEYNNETEN
     NENQEFQNDN YDSDFEPTAD AEIESSDALN KDSLTDELPM DVGWDEYISA GPSTSSGPAP
     DNDTIYQGST SETLHDYLMW QLRLTRFSPT DEAIAIAIVE AINDDGYLTL STEDICDSIG
     EGSDGLAVEL DEVEAVLKRI QVFDPIGIAA RNFPECLLIQ LNQFAKDTPW LAQTKEIVQQ
     HIELLAARDY RTLMKKTKLK EEELKEIMTL IHTLNPKPAD SINTEQPEYV IPDVSVKKIK
     GRWVVELNSD SMPKIRVNDQ YAAMSRSVKS SEDSQFIRSH LQEAKWFIKS LESRNDTLLK
     VANCIVQQQQ AFFEHGDEAM KPMVLNDVAE MVEMHESTIS RVTTQKFMHT PRGIYELKFF
     FSSHVSTENG GECSSTAIRA LIKKLVAAEN QTKPLSDSKI ADILAEQGIN VARRTIAKYR
     ESLSIPPSNQ RKSLI
//
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