ID R5LRB2_9CLOT Unreviewed; 149 AA.
AC R5LRB2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=BN500_01025 {ECO:0000313|EMBL:CCY81800.1};
OS Clostridium sp. CAG:149.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262776 {ECO:0000313|EMBL:CCY81800.1, ECO:0000313|Proteomes:UP000017912};
RN [1] {ECO:0000313|EMBL:CCY81800.1, ECO:0000313|Proteomes:UP000017912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:149 {ECO:0000313|Proteomes:UP000017912};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCY81800.1}.
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DR EMBL; CAYX010000065; CCY81800.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LRB2; -.
DR Proteomes; UP000017912; Unassembled WGS sequence.
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:UP000017912};
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_00637}.
FT DOMAIN 45..149
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 149 AA; 16517 MW; 6D5BA76EAB422E5D CRC64;
MQKVMEEKRR EPEWMKMEIE SRSENEEFAR VAVAVFLSRL DPTVEEMDDI KTAVSEAVTN
AVIHGYQGGE GTIYIETGIA GQEATVIVRD LGVGIPDIEK AMEPMYTTDL SGERSGMGFS
FMEAFMDEVK VESEPGKGTT VTLKKTVGR
//
