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Entry: A0A0B6WYQ7_9BACT
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ID   A0A0B6WYQ7_9BACT        Unreviewed;       747 AA.
AC   A0A0B6WYQ7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=PYK22_01283 {ECO:0000313|EMBL:CDM65285.1};
OS   Pyrinomonas methylaliphatogenes.
OC   Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC   Pyrinomonadaceae; Pyrinomonas.
OX   NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM65285.1, ECO:0000313|Proteomes:UP000031518};
RN   [1] {ECO:0000313|EMBL:CDM65285.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM65285.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Stott M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDM65285.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM65285.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA   Stott M.B.;
RT   "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT   K22T.";
RL   Submitted (JAN-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}.
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DR   EMBL; CBXV010000004; CDM65285.1; -; Genomic_DNA.
DR   RefSeq; WP_060635411.1; NZ_CBXV010000004.1.
DR   AlphaFoldDB; A0A0B6WYQ7; -.
DR   STRING; 454194.PYK22_01283; -.
DR   Proteomes; UP000031518; Unassembled WGS sequence.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
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   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:CDM65285.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:CDM65285.1}.
FT   DOMAIN          628..739
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF13581"
SQ   SEQUENCE   747 AA;  84345 MW;  65EFC172BFA4DF2A CRC64;
     MSSEAQNRRH PILGHVARAD FVGRDAELQR IVNLARRETA ERGLFLLAPP GAGLSELLRQ
     SYDALFHDEL AIPIYFAWSL HDRTASAAAR HFLQTFLLQL TAYRRREPAL IDAHPTLNDL
     LQLAAPSDYV WLEQLLESYE QVRADGDERQ LVRLCLSAPQ RAAAGGVTTV LLFDDVHLAE
     HLSGETALGA EVARACIRAG TPFVIAGLRR RVLEVVSAAD MLFEQTGTLH LDLLSEADAR
     SLIERWAARR QIRLNGATCD LIVQELKGRP FFLTALLRAA QEAKEDLDNF LACQRLYVDE
     LLGGRINRRF AEVWERIVPN GAMRRAFVRA LYETANAAQG QSPVEAWLKR LSMSSDELQR
     TLRQMHAQEL INFSGTFIEV ADDTVWRDYL EITYRLEVAA ERRALVVADT LLSLLMRAPQ
     TMARRYRSEA ALHLRELLAR FNCQRVPASL LHYDRFSRMY KGMEPEAIAS ALDAETDLVL
     LPQIIHTAPC LAFHQSFERL CEEAQCVVAH GFDAGQYAEA NQIVWLAAEI EAKVEVGRAV
     AEMWHNRLVE LARSCGFKRF RVWLVAPAGF SAEACEFLRE REAYGSNRQQ LEFLTARLSV
     PLSKSTTEAQ ADEFEMVIPI GEDTELIAAH TVEQIARRLN FEPEAINQIK VALVEACLNV
     AEHSLSPERK IYQRFRAESD RLVITVWSRG VAFHGEPNNN GKQTSGRSKR GLGLKLIRTL
     MDEVEFKRVD DGACLRMTKY LHPRTSS
//
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