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Database: UniProt
Entry: G2G116_9FIRM
LinkDB: G2G116_9FIRM
Original site: G2G116_9FIRM 
ID   G2G116_9FIRM            Unreviewed;       114 AA.
AC   G2G116;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Anti-sigma F factor antagonist {ECO:0000256|ARBA:ARBA00020784, ECO:0000256|RuleBase:RU003749};
DE   AltName: Full=Stage II sporulation protein {ECO:0000256|RuleBase:RU003749};
GN   Name=spoIIAA {ECO:0000313|EMBL:EGW36394.1};
GN   ORFNames=DOT_5702 {ECO:0000313|EMBL:EGW36394.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW36394.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW36394.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW36394.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
CC   -!- FUNCTION: In the phosphorylated form it could act as an anti-anti-sigma
CC       factor that counteracts SpoIIAB and thus releases sigma f from
CC       inhibition. {ECO:0000256|ARBA:ARBA00001976}.
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC       {ECO:0000256|ARBA:ARBA00009013, ECO:0000256|RuleBase:RU003749}.
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:EGW36394.1}.
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DR   EMBL; AGAF01000257; EGW36394.1; -; Genomic_DNA.
DR   RefSeq; WP_009624349.1; NZ_AGAF01000257.1.
DR   AlphaFoldDB; G2G116; -.
DR   PATRIC; fig|913865.3.peg.5236; -.
DR   eggNOG; COG1366; Bacteria.
DR   OrthoDB; 9796601at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
DR   GO; GO:0043856; F:anti-sigma factor antagonist activity; IEA:InterPro.
DR   GO; GO:0045152; F:antisigma factor binding; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd07043; STAS_anti-anti-sigma_factors; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR003658; Anti-sigma_ant.
DR   InterPro; IPR014237; Anti-sigma_F_ant.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR00377; ant_ant_sig; 1.
DR   NCBIfam; TIGR02886; spore_II_AA; 1.
DR   PANTHER; PTHR33495:SF2; ANTI-SIGMA FACTOR ANTAGONIST TM_1081-RELATED; 1.
DR   PANTHER; PTHR33495; ANTI-SIGMA FACTOR ANTAGONIST TM_1081-RELATED-RELATED; 1.
DR   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT   DOMAIN          1..114
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
SQ   SEQUENCE   114 AA;  12904 MW;  EDCA8224CA600E07 CRC64;
     MNLEKKIERL TLLLRLDGEL DMHTASMVRQ AIDSEIEKRG IRTVILNLQD VRFIDSSGLG
     VILGRYKKLL SLGGKLKITN VPPHIYKIME LSGLPKIINF YLDEAHAYEE GRGA
//
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