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Database: UniProt
Entry: A0A0X3T8D5_9GAMM
LinkDB: A0A0X3T8D5_9GAMM
Original site: A0A0X3T8D5_9GAMM 
ID   A0A0X3T8D5_9GAMM        Unreviewed;       502 AA.
AC   A0A0X3T8D5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=AVO41_06240 {ECO:0000313|EMBL:KUJ72035.1};
OS   Thiomicrospira sp. WB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=1685380 {ECO:0000313|EMBL:KUJ72035.1, ECO:0000313|Proteomes:UP000053531};
RN   [1] {ECO:0000313|EMBL:KUJ72035.1, ECO:0000313|Proteomes:UP000053531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WB1 {ECO:0000313|EMBL:KUJ72035.1,
RC   ECO:0000313|Proteomes:UP000053531};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-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}.
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:KUJ72035.1}.
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DR   EMBL; LQBN01000002; KUJ72035.1; -; Genomic_DNA.
DR   RefSeq; WP_068584310.1; NZ_LQBN01000002.1.
DR   AlphaFoldDB; A0A0X3T8D5; -.
DR   STRING; 1685380.AVO41_06240; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000053531; 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:UP000053531};
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          122..324
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          339..497
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          60..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  57518 MW;  C1359BD23ED1816A CRC64;
     MALMPGLQLN MGQQLKLTPQ LQQSIKILQY SALEVQQTIA TTLETNFMLE LDDEFVEEEL
     ADEPRDEASD EQTHADEKEI DLESADKLDD DMQVDCEWEE VYTDIPVATR SASLDSEYTA
     PENYTAAELS LAEKLYWQAD IYPWPNPDNQ EVPDQAVIAS YLIDEIDDEG YLKTPLEQIE
     AAIKKNEPEL AISVEQLEQV LAVIWEFEPT GVGARDLSEC LLLQLKPLKQ TPYVVTARKI
     IEDHFDLLSV RDYKRLKKIY LLDDDDLMEV IHVIQALSPR PGRAYASTQN ELVIPDLRLH
     RTATGYMVEL NQEAFPRLSI NRAYVDMAND LQGQSGESKQ IKEQLFEAKS LIKSIQSRGE
     TLLRVGRYIV EKQARFFEEG EQAMQPMVLR DLAEALDLHE STISRATNQK YIQTPRGTFE
     LKYFFSTGVS QYGSDDQSAI AIKSHIKQLI ENEDPKKPLS DNKLMQLLED KDISVARRTI
     AKYREAMHIP SSSERKRMNQ YR
//
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