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Database: UniProt
Entry: A8T965_9VIBR
LinkDB: A8T965_9VIBR
Original site: A8T965_9VIBR 
ID   A8T965_9VIBR            Unreviewed;       488 AA.
AC   A8T965;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   13-SEP-2023, entry version 65.
DE   RecName: Full=RNA polymerase sigma-54 factor {ECO:0000256|ARBA:ARBA00019942, ECO:0000256|PIRNR:PIRNR000774};
GN   ORFNames=AND4_13400 {ECO:0000313|EMBL:EDP58159.1};
OS   Vibrio sp. AND4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP58159.1, ECO:0000313|Proteomes:UP000005159};
RN   [1] {ECO:0000313|EMBL:EDP58159.1, ECO:0000313|Proteomes:UP000005159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AND4 {ECO:0000313|EMBL:EDP58159.1,
RC   ECO:0000313|Proteomes:UP000005159};
RX   PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA   Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA   Milton D.L., Gonzalez J.M., Pinhassi J.;
RT   "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT   starvation.";
RL   PLoS Biol. 8:E1000358-E1000358(2010).
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:EDP58159.1}.
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DR   EMBL; ABGR01000014; EDP58159.1; -; Genomic_DNA.
DR   RefSeq; WP_009843575.1; NZ_ABGR01000014.1.
DR   AlphaFoldDB; A8T965; -.
DR   OrthoDB; 9814402at2; -.
DR   Proteomes; UP000005159; 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..316
FT                   /note="RNA polymerase sigma factor 54 core-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04963"
FT   DOMAIN          328..486
FT                   /note="RNA polymerase sigma factor 54 DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04552"
FT   REGION          49..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  54763 MW;  9BAA4A967E9F616E CRC64;
     MKPSLQLKLG QQLAMTPQLQ QAIRLLQLST LDLQQEIQEA LDSNPLLEVE EGHEEPQKND
     EDKSASESAD SSASEASEPD LPDSSDLIEK SEISSELEID TTWDDVYSAN TGSTGIALDD
     DMPVYQGETT ESLQDYLMWQ LDLTPFSDTD RTIALALIDA IDDYGYLTLS PEEIHESFDN
     EEVELDEVEA VRKRIQQFDP LGVASRNLQE CLLLQLATFP EDTPWLAEAK MVLSNHIDQL
     GNRDYKLVIK ETKLKEADLR AVLKLIQQLD PRPGSRITPD DTEYVIPDVS VFKDNGKWTV
     SINPDSIPKL KVNQQYAQLG KGNSADSQYI RSNLQEAKWL IKSLESRNET LLKVARCIVE
     HQQEFFEYGE EAMKPMVLND VALDVDMHES TISRVTTQKF MHTPRGIFEL KYFFSSHVST
     DNGGECSSTA IRALIKKLVA AENTAKPLSD SKIAALLADQ GIQVARRTIA KYRESLGIAP
     SSQRKRLL
//
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