SP2AB_GEOSE
ID SP2AB_GEOSE Reviewed; 146 AA.
AC O32727;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Anti-sigma F factor {ECO:0000255|HAMAP-Rule:MF_00637};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_00637};
DE AltName: Full=Stage II sporulation protein AB {ECO:0000255|HAMAP-Rule:MF_00637};
GN Name=spoIIAB {ECO:0000255|HAMAP-Rule:MF_00637};
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: Binds to sigma F and blocks its ability to form an RNA
CC polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine
CC residue. This phosphorylation may enable SpoIIAA to act as an anti-
CC anti-sigma factor that counteracts SpoIIAB and thus releases sigma F
CC from inhibition. {ECO:0000255|HAMAP-Rule:MF_00637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00637};
CC -!- INTERACTION:
CC O32727; O32726: spoIIAA; NbExp=4; IntAct=EBI-1033242, EBI-1039369;
CC O32727; O32728; NbExp=5; IntAct=EBI-1033242, EBI-1033248;
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000255|HAMAP-Rule:MF_00637}.
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DR EMBL; L47360; AAB81193.1; -; Genomic_DNA.
DR PDB; 1L0O; X-ray; 2.90 A; A/B=1-136.
DR PDB; 1TH8; X-ray; 2.40 A; A=1-136.
DR PDB; 1THN; X-ray; 2.50 A; A/C=1-136.
DR PDB; 1TID; X-ray; 2.50 A; A/C=1-136.
DR PDB; 1TIL; X-ray; 2.70 A; A/C/E=1-136.
DR PDBsum; 1L0O; -.
DR PDBsum; 1TH8; -.
DR PDBsum; 1THN; -.
DR PDBsum; 1TID; -.
DR PDBsum; 1TIL; -.
DR AlphaFoldDB; O32727; -.
DR SMR; O32727; -.
DR IntAct; O32727; 2.
DR EvolutionaryTrace; O32727; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
DR GO; GO:0030436; P:asexual sporulation; IEA:UniProtKB-UniRule.
DR GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00637; Anti_sigma_F; 1.
DR InterPro; IPR010194; Anti-sigma_F.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR01925; spIIAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding;
KW Serine/threonine-protein kinase; Sporulation; Transferase.
FT CHAIN 1..146
FT /note="Anti-sigma F factor"
FT /id="PRO_0000203560"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1TH8"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1TH8"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1TH8"
FT HELIX 34..53
FT /evidence="ECO:0007829|PDB:1TH8"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1TID"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:1TH8"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1TH8"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1TH8"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:1THN"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:1TH8"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1TH8"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1TH8"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:1TH8"
SQ SEQUENCE 146 AA; 16239 MW; B3F1BD38A9044416 CRC64;
MRNEMHLQFS ARSENESFAR VTVAAFVAQL DPTTDELTEI KTVVSEAVTN AIIHGYNNDP
NGIVSISVII EDGVVHLTVR DEGVGIPDIE EARQPLFTTK PELERSGMGF TIMENFMDEV
IVESEVNKGT TVYLKKAYCE KQTLCN
