ID I4EX49_9ACTN Unreviewed; 312 AA.
AC I4EX49;
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_2533 {ECO:0000313|EMBL:CCH87962.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87962.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87962.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87962.1,
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; CCH87962.1; -; Genomic_DNA.
DR RefSeq; WP_014740554.1; NC_017955.1.
DR AlphaFoldDB; I4EX49; -.
DR STRING; 477641.MODMU_2533; -.
DR KEGG; mmar:MODMU_2533; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_072253_0_0_11; -.
DR OMA; AVANRCY; -.
DR OrthoDB; 4350801at2; -.
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:SF3; STAS DOMAIN-CONTAINING PROTEIN; 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:CCH87962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CCH87962.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000313|EMBL:CCH87962.1}.
FT DOMAIN 17..160
FT /note="MEDS"
FT /evidence="ECO:0000259|Pfam:PF14417"
FT DOMAIN 206..309
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 312 AA; 34719 MW; 36190783383B80BB CRC64;
MTSMRPTGEW DGTTFAHEAF LFATDQEVLD RIVPFTVEGL SRGEPVLVVA GKRVRRLLAA
ELGQDVRRLA TFAAAETWWR GGHGTLHAYD RDLRTLRSAA PTWRLVAEPV WLAREDGREW
SRFEAVANRC YAAMPYYSLC LHDRRRLPTS VLDAVVRTHP LTWSGHAPVE AAAYEDPTRF
LRSVQPEWDA RPGHSAVWTV TAPQEARRAL AAAVIDGWRE RADDVVLATH ELLTNALRVA
PFVEVAFWTD HETLVVEVAD TGPGLPDETR GYVPPAADLA GGRGMWLAWS LADDAAVASS
PTGTAIRLYF RR
//
