ID D9T3W1_MICAI Unreviewed; 149 AA.
AC D9T3W1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Micau_6216 {ECO:0000313|EMBL:ADL49709.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL49709.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL49709.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002162; ADL49709.1; -; Genomic_DNA.
DR RefSeq; WP_013289306.1; NC_014391.1.
DR AlphaFoldDB; D9T3W1; -.
DR STRING; 644283.Micau_6216; -.
DR KEGG; mau:Micau_6216; -.
DR eggNOG; COG2172; Bacteria.
DR HOGENOM; CLU_090336_5_1_11; -.
DR OrthoDB; 3473090at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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 SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:ADL49709.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000313|EMBL:ADL49709.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 15..134
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
SQ SEQUENCE 149 AA; 15376 MW; 501136FF83560FC7 CRC64;
MSTGPAERSW CVVVPHDPTG ARLARHRLAD ELTGVVPPVL VADLVAVLAE LVGNAVRHAD
ALPGGVVRVA WRLRPTEQGP SVELRVTDGG SGAGPCMRTA SPDAADGRGL HIVAGLASGW
GVERDGLGQS VWARFDPVPA QRTDLVAAG
//