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Database: UniProt
Entry: A0A077AWX7_9PROT
LinkDB: A0A077AWX7_9PROT
Original site: A0A077AWX7_9PROT 
ID   A0A077AWX7_9PROT        Unreviewed;       453 AA.
AC   A0A077AWX7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=ID47_06595 {ECO:0000313|EMBL:AIK96484.1};
OS   Candidatus Paracaedibacter acanthamoebae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales;
OC   Candidatus Paracaedibacteraceae; Paracaedibacter.
OX   NCBI_TaxID=91604 {ECO:0000313|EMBL:AIK96484.1, ECO:0000313|Proteomes:UP000028926};
RN   [1] {ECO:0000313|EMBL:AIK96484.1, ECO:0000313|Proteomes:UP000028926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRA3 {ECO:0000313|EMBL:AIK96484.1};
RA   Wang Z., Wu M.;
RT   "Comparative genomic insights into amoeba endosymbionts belonging to the
RT   families of Holosporaceae and Candidatus Midichloriaceae within
RT   Rickettsiales.";
RL   Submitted (JUL-2014) 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; CP008941; AIK96484.1; -; Genomic_DNA.
DR   RefSeq; WP_038464931.1; NZ_CP008941.1.
DR   AlphaFoldDB; A0A077AWX7; -.
DR   STRING; 91604.ID47_06595; -.
DR   KEGG; paca:ID47_06595; -.
DR   eggNOG; COG1508; Bacteria.
DR   HOGENOM; CLU_020569_1_1_5; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000028926; 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:UP000028926};
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          91..272
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          290..446
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
SQ   SEQUENCE   453 AA;  51515 MW;  FDE02455AFDE1DD5 CRC64;
     MKTQLHTYLK QSQQLNLSPQ MQQSLRILQL STVEVQELID QSLLENPFLE QESAHTSFAA
     PQDSLIDDNP YTSYWKEQQV RIPNSDVTHD TNAQPSTLKS HLTQQLFITT PNQKFRDIGT
     YLIDHIDEDG YLRLPPDDRT LQTCGPEILN QAINLIQSLD PVGVGARTLS ECLALQLKDR
     GLYNETYAAI LDNLHLLIEK GPLALAQKCA LDVETFRAKM DLIKTLSPQP GLAFSPTETT
     IYITPDLLFR RYNGQWIAEL NKEAYPRLFI DEKSFTAVIN KCQSIDDKIY MNKQISSANW
     LVKSLEQRAI TMLKVANAII RHQIHFLNRG HNYLTPLKLK DIATEVDIHE STVSRAVTGK
     YAATPFGVIE LKSFFSTALN EEQPTLSNKT IQLQIKKLID MESKSSPLSD DQLVSTLKTY
     GISVARRTVT KYRESLQIPS SYERKKMARV LNF
//
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