SP2AA_LYSSH
ID SP2AA_LYSSH Reviewed; 117 AA.
AC O32723;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Anti-sigma F factor antagonist;
DE AltName: Full=Stage II sporulation protein AA;
GN Name=spoIIAA;
OS Lysinibacillus sphaericus (Bacillus sphaericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2362;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), AND PHOSPHORYLATION AT SER-58.
RX PubMed=11470435; DOI=10.1016/s0969-2126(01)00623-2;
RA Seavers P.R., Lewis R.J., Brannigan J.A., Verschueren K.H., Murshudov G.N.,
RA Wilkinson A.J.;
RT "Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated
RT and unphosphorylated forms.";
RL Structure 9:605-614(2001).
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; L47359; AAB81189.1; -; Genomic_DNA.
DR RefSeq; WP_025114066.1; NZ_PEKE01000001.1.
DR PDB; 1H4X; X-ray; 1.16 A; A/B=1-117.
DR PDB; 1H4Y; X-ray; 1.61 A; A/B=1-117.
DR PDB; 1H4Z; X-ray; 2.74 A; A=1-117.
DR PDBsum; 1H4X; -.
DR PDBsum; 1H4Y; -.
DR PDBsum; 1H4Z; -.
DR AlphaFoldDB; O32723; -.
DR SMR; O32723; -.
DR STRING; 1421.A2J09_02155; -.
DR DrugBank; DB04522; Dexfosfoserine.
DR iPTMnet; O32723; -.
DR GeneID; 29441082; -.
DR PATRIC; fig|1421.29.peg.4416; -.
DR OrthoDB; 1864829at2; -.
DR EvolutionaryTrace; O32723; -.
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..117
FT /note="Anti-sigma F factor antagonist"
FT /id="PRO_0000194202"
FT DOMAIN 2..115
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11470435"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1H4X"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:1H4X"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:1H4X"
FT STRAND 43..55
FT /evidence="ECO:0007829|PDB:1H4X"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:1H4X"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1H4X"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1H4X"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:1H4X"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1H4X"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1H4X"
SQ SEQUENCE 117 AA; 13043 MW; C3BF8A70AB9340A1 CRC64;
MHFQLEMVTR ETVVIRLFGE LDHHAVEQIR AKISAAIFQG TVTTIIWNLE GLSFMDSSGV
GLVLGRMREL EAVAGRTILL NPSPTMRKVF QFSGLGPWMM DATEEQAIDR VRGIVNG
