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Database: UniProt
Entry: A0A2P8PZD5_9ACTN
LinkDB: A0A2P8PZD5_9ACTN
Original site: A0A2P8PZD5_9ACTN 
ID   A0A2P8PZD5_9ACTN        Unreviewed;       135 AA.
AC   A0A2P8PZD5;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=C6Y14_31215 {ECO:0000313|EMBL:PSM39356.1};
OS   Streptomyces dioscori.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=2109333 {ECO:0000313|EMBL:PSM39356.1, ECO:0000313|Proteomes:UP000240429};
RN   [1] {ECO:0000313|EMBL:PSM39356.1, ECO:0000313|Proteomes:UP000240429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A217 {ECO:0000313|EMBL:PSM39356.1,
RC   ECO:0000313|Proteomes:UP000240429};
RA   Zhikuan W.;
RT   "Streptomyces dioscori sp. nov., a novel endophytic actinobacterium
RT   isolated from bulbil of Dioscorea bulbifera L.";
RL   Submitted (MAR-2018) 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:PSM39356.1}.
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DR   EMBL; PYBJ01000025; PSM39356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8PZD5; -.
DR   OrthoDB; 3852626at2; -.
DR   Proteomes; UP000240429; 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   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   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240429};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          16..129
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
FT   REGION          83..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   135 AA;  14611 MW;  06EC2BBE44EC3B7E CRC64;
     MSRVIHTEGD VAEWTFPAEP GAVRTARAVV RGQLRAWGLE SLSDVTALLV SELVTNSLRH
     ATGPIGVRLV RPSGLLDGLL VEVSDPLPDP PRERSAQPDD ETGRGLRLVA DAARRWGTRP
     GETGKTVWFE LALPD
//
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