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Database: UniProt
Entry: A0A286GC31_9PROT
LinkDB: A0A286GC31_9PROT
Original site: A0A286GC31_9PROT 
ID   A0A286GC31_9PROT        Unreviewed;       512 AA.
AC   A0A286GC31;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=SAMN05421508_102493 {ECO:0000313|EMBL:SOD92554.1};
OS   Caenispirillum bisanense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Caenispirillum.
OX   NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD92554.1, ECO:0000313|Proteomes:UP000219621};
RN   [1] {ECO:0000313|EMBL:SOD92554.1, ECO:0000313|Proteomes:UP000219621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 140 {ECO:0000313|EMBL:SOD92554.1,
RC   ECO:0000313|Proteomes:UP000219621};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OCNJ01000002; SOD92554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286GC31; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000219621; 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   Reference proteome {ECO:0000313|Proteomes:UP000219621};
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          143..330
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          346..503
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          50..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  56432 MW;  8E11B3E116089BF3 CRC64;
     MVLAPSLHLR QTQSLVMTPQ LQQAIKLLQL SNIELTAYVE QELERNPLLE RAEPRDVAGA
     GEDRYDDRRD AGEGVLVDSP DGRAGSEAPL DVEIDNSYDA QEYESGPAAP EGVAAAGAEG
     FADDWSNVGS GGRRDFMDED GGYENTLAGG VSLRDHLVDQ LACDVPEGAD RLIGQAFIDS
     LDDNGYLTVT VEEMAEAMGA PVERVRRVLD RLQRFDPPGL FARDLSECLA LQLREKDRLD
     PCMQALLANL DLLARRDVPQ LLKVCGVDAE DLAEMVAEIR ACDPRPALRF TDVPAQPVVP
     DVLMRPAPDG GWHVELNTDA LPRVLVNHRY YALVSKAARS KEDKGFVAEN FQTASWLVKA
     LDQRANTILK VAVEIVRQQD AFFVHGISAL RPLILRDIAT AIEMHESTVS RVTSNKYIAT
     PRGIFELKYF FTQAIAGADG EAHSAEAVRH RIRALIDAES ADDVLSDDTL VALLKKEGID
     IARRTVAKYR EGMKIASSVQ RRREKRMKLT QA
//
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