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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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