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Database: UniProt
Entry: A0A0F5MZG0_9MYCO
LinkDB: A0A0F5MZG0_9MYCO
Original site: A0A0F5MZG0_9MYCO 
ID   A0A0F5MZG0_9MYCO        Unreviewed;       316 AA.
AC   A0A0F5MZG0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=WR43_06245 {ECO:0000313|EMBL:KKC00156.1};
OS   Mycolicibacter arupensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=342002 {ECO:0000313|EMBL:KKC00156.1, ECO:0000313|Proteomes:UP000034416};
RN   [1] {ECO:0000313|Proteomes:UP000034416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUC1 {ECO:0000313|Proteomes:UP000034416};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium arupense GUC1.";
RL   Submitted (APR-2015) 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}.
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:KKC00156.1}.
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DR   EMBL; LASW01000017; KKC00156.1; -; Genomic_DNA.
DR   RefSeq; WP_046188715.1; NZ_MVHH01000001.1.
DR   AlphaFoldDB; A0A0F5MZG0; -.
DR   STRING; 342002.BST15_01105; -.
DR   PATRIC; fig|342002.3.peg.1589; -.
DR   OrthoDB; 4088450at2; -.
DR   Proteomes; UP000034416; Unassembled WGS sequence.
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};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          13..158
FT                   /note="MEDS"
FT                   /evidence="ECO:0000259|Pfam:PF14417"
FT   DOMAIN          199..310
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   316 AA;  33870 MW;  35F863154DF93B5C CRC64;
     MAVAAGEDRD SFRHIALTYG SPQEYLDYLV TFVGDGVAEG VPVLIAVPGP SLALLRSALS
     PGTFDAVTAV DMSRAGRNPG HILGGVFGAF AARHRSSPVK MVGEQIWHGR SPQEYSACLQ
     HEALVNEAFA GRDLTVVCPF DATHVDSATL VDAEITHPRV SRGGRGDRAS ATFAPQAAWE
     RCNEPLPGNP TAASYAVHRL ADLAGARQFC ARYARWFGLT ADAIADLQLI VNELATNSLQ
     HGRRPITLLL WESAGQLVCQ VRDAGHLTDR LAGRRPIVGD VDDGRGLYVV NATADLVRIH
     AAPTGTTVQA HLRMRR
//
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