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SP2AA_PAEPO
ID   SP2AA_PAEPO             Reviewed;         117 AA.
AC   O32720;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Anti-sigma F factor antagonist;
DE   AltName: Full=Stage II sporulation protein AA;
GN   Name=spoIIAA;
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343
RC   / NRRL B-4317 / VKM B-514;
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   -!- 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; L47358; AAB81184.1; -; Genomic_DNA.
DR   AlphaFoldDB; O32720; -.
DR   SMR; O32720; -.
DR   STRING; 1052684.PPM_2994; -.
DR   eggNOG; COG1366; Bacteria.
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   3: Inferred from homology;
KW   Phosphoprotein; Sporulation.
FT   CHAIN           1..117
FT                   /note="Anti-sigma F factor antagonist"
FT                   /id="PRO_0000194205"
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"
SQ   SEQUENCE   117 AA;  13342 MW;  7D66D2AA8D788B0A CRC64;
     MNLQIEMEHH RGVLIVRLSG ELDHHTSDMV RMQMDEAIQR RQCEHIVLSL KNLQFMDSSG
     LGVILGRYKL INQKGGEMAV CDVNPPVHRL LDMSGLFKIM PIYDNEVNAL TELEVVS
 
 
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