ID I3EA48_BACMM Unreviewed; 146 AA.
AC I3EA48;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Anti-sigma F factor {ECO:0000256|HAMAP-Rule:MF_00637};
DE EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_00637};
DE AltName: Full=Stage II sporulation protein AB {ECO:0000256|HAMAP-Rule:MF_00637};
GN Name=spoIIAB {ECO:0000256|HAMAP-Rule:MF_00637,
GN ECO:0000313|EMBL:AIE60611.1};
GN ORFNames=BMMGA3_11075 {ECO:0000313|EMBL:AIE60611.1};
OS Bacillus methanolicus (strain MGA3 / ATCC 53907).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=796606 {ECO:0000313|EMBL:AIE60611.1, ECO:0000313|Proteomes:UP000027602};
RN [1] {ECO:0000313|EMBL:AIE60611.1, ECO:0000313|Proteomes:UP000027602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGA3 / ATCC 53907 {ECO:0000313|Proteomes:UP000027602};
RX PubMed=25758049;
RA Irla M., Neshat A., Brautaset T., Ruckert C., Kalinowski J., Wendisch V.F.;
RT "Transcriptome analysis of thermophilic methylotrophic Bacillus
RT methanolicus MGA3 using RNA-sequencing provides detailed insights into its
RT previously uncharted transcriptional landscape.";
RL BMC Genomics 16:73-73(2015).
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:0000256|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:0000256|ARBA:ARBA00001433, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000775,
CC ECO:0000256|HAMAP-Rule:MF_00637};
CC -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000256|ARBA:ARBA00037972, ECO:0000256|HAMAP-Rule:MF_00637}.
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DR EMBL; CP007739; AIE60611.1; -; Genomic_DNA.
DR RefSeq; WP_004435412.1; NZ_CP007739.1.
DR AlphaFoldDB; I3EA48; -.
DR STRING; 796606.BMMGA3_11075; -.
DR KEGG; bmet:BMMGA3_11075; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_11_0_9; -.
DR OrthoDB; 9768808at2; -.
DR Proteomes; UP000027602; Chromosome.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 NCBIfam; TIGR01925; spIIAB; 1.
DR PANTHER; PTHR35526:SF7; ANTI-SIGMA F FACTOR; 1.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00637};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00637};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00637};
KW Reference proteome {ECO:0000313|Proteomes:UP000027602};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_00637};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969, ECO:0000256|HAMAP-
KW Rule:MF_00637};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00637, ECO:0000313|EMBL:AIE60611.1}.
FT DOMAIN 35..140
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 146 AA; 16357 MW; A97029763903A9B7 CRC64;
MKNEMNLQFS ALSQNESFAR VTVAAFIAQL DPTMDELTEI KTVVSEAVTN AIIHGYENDP
KGIVYISVSI EDEIVDMTIR DEGVGIKDIE EARQPLFTTK PDLERSGMGF TIMENFMDEV
QVHSQPGKGT EVRLRKLLSK SKMLCN
//
