ID   SP2AA_GEOSE             Reviewed;         116 AA.
AC   O32726;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Anti-sigma F factor antagonist;
DE   AltName: Full=Stage II sporulation protein AA;
GN   Name=spoIIAA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC   / NCTC 10339 / R-35646 / VKM B-510;
RX   PubMed=9266669; DOI=10.1016/s0378-1119(97)00096-6;
RA   Park S.G., Yudkin M.D.;
RT   "Sequencing and phylogenetic analysis of the spoIIA operon from diverse
RT   Bacillus and Paenibacillus species.";
RL   Gene 194:25-33(1997).
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:0000250}.
CC   -!- INTERACTION:
CC       O32726; O32727: spoIIAB; NbExp=4; IntAct=EBI-1039369, EBI-1033242;
CC   -!- PTM: Phosphorylated by SpoIIAB on a serine residue. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anti-sigma-factor antagonist family.
CC       {ECO:0000305}.
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DR   EMBL; L47360; AAB81192.1; -; Genomic_DNA.
DR   PDB; 1TH8; X-ray; 2.40 A; B=1-116.
DR   PDB; 1THN; X-ray; 2.50 A; B/D=1-116.
DR   PDB; 1TID; X-ray; 2.50 A; B/D=1-116.
DR   PDB; 1TIL; X-ray; 2.70 A; B/D/F=1-116.
DR   PDBsum; 1TH8; -.
DR   PDBsum; 1THN; -.
DR   PDBsum; 1TID; -.
DR   PDBsum; 1TIL; -.
DR   AlphaFoldDB; O32726; -.
DR   SMR; O32726; -.
DR   IntAct; O32726; 1.
DR   EvolutionaryTrace; O32726; -.
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   Gene3D; 3.30.750.24; -; 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   Pfam; PF01740; STAS; 1.
DR   SUPFAM; SSF52091; SSF52091; 1.
DR   TIGRFAMs; TIGR00377; ant_ant_sig; 1.
DR   TIGRFAMs; TIGR02886; spore_II_AA; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Sporulation.
FT   CHAIN           1..116
FT                   /note="Anti-sigma F factor antagonist"
FT                   /id="PRO_0000194203"
FT   DOMAIN          3..113
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   STRAND          13..23
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   HELIX           24..39
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   STRAND          45..56
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   HELIX           58..73
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   HELIX           85..93
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:1TH8"
FT   HELIX           106..112
FT                   /evidence="ECO:0007829|PDB:1TH8"
SQ   SEQUENCE   116 AA;  12859 MW;  A6E2EAB055B27C93 CRC64;
     MSLAIDLEVK QDELIVRLSG ELDHHTAENC MNKCRMCLEK RAIRHIVLNL GQLTFMDSSG
     LGVILGRYKQ IKNVGGQMVV CAVSPAVKRL FDMSGLFKII RVEADEQFAL QALGVA