ID I4EQL6_9ACTN Unreviewed; 319 AA.
AC I4EQL6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=MODMU_0216 {ECO:0000313|EMBL:CCH85679.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH85679.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH85679.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH85679.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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};
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 -!- SIMILARITY: Belongs to the anti-sigma-factor family.
CC {ECO:0000256|ARBA:ARBA00037972}.
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DR EMBL; FO203431; CCH85679.1; -; Genomic_DNA.
DR RefSeq; WP_014738295.1; NC_017955.1.
DR AlphaFoldDB; I4EQL6; -.
DR STRING; 477641.MODMU_0216; -.
DR KEGG; mmar:MODMU_0216; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_072253_0_0_11; -.
DR OMA; QLVWPGR; -.
DR OrthoDB; 4088450at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd16936; HATPase_RsbW-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR025847; MEDS_domain.
DR InterPro; IPR047718; RsbA-like_anti_sig.
DR NCBIfam; NF041045; RsbA_anti_sig; 1.
DR PANTHER; PTHR35526; ANTI-SIGMA-F FACTOR RSBW-RELATED; 1.
DR PANTHER; PTHR35526:SF1; SERINE-PROTEIN KINASE RSBW; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF14417; MEDS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000313|EMBL:CCH85679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CCH85679.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000313|EMBL:CCH85679.1}.
FT DOMAIN 5..155
FT /note="MEDS"
FT /evidence="ECO:0000259|Pfam:PF14417"
FT DOMAIN 199..315
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 319 AA; 34690 MW; ED8EF4FC5A4F9FFA CRC64;
MDGAHRALIG ASDPELVDGT VAFVRDALDA GEQVVVVCTD PTAELLQKAL ADLPQVAWAE
WGEVYGHGPA AAVTAVRRLG ERHRTPGNRV VRVVLEPLAG PDRDTWREWQ RYDAVLDHQL
DEADRLGEEP LLVLCLCDTR RVPAELVQAA RHTHPSLQVD GAAVVNPAHV DAAEYLTSLP
VPVEPLEATQ PLVRADSVRD LRGLRRDLAA RAAEARLPAG SESALEDFLL AVDEMTTNAL
RHGRPPVDLR LWVDDRRLVC TVTDRGAGLQ DPFIGYGPAH GDDLSLGGMG LWLARQLCDH
VDISVADQGV RVRLTTVLH
//
