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Database: UniProt
Entry: W0RF59_9BACT
LinkDB: W0RF59_9BACT
Original site: W0RF59_9BACT 
ID   W0RF59_9BACT            Unreviewed;       660 AA.
AC   W0RF59;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:AHG88975.1};
GN   ORFNames=J421_1438 {ECO:0000313|EMBL:AHG88975.1};
OS   Gemmatirosa kalamazoonensis.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG88975.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG88975.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG88975.1,
RC   ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
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};
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DR   EMBL; CP007128; AHG88975.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RF59; -.
DR   STRING; 861299.J421_1438; -.
DR   KEGG; gba:J421_1438; -.
DR   PATRIC; fig|861299.3.peg.1461; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_391702_0_0_0; -.
DR   InParanoid; W0RF59; -.
DR   Proteomes; UP000019151; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AHG88975.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000019151};
KW   Transferase {ECO:0000313|EMBL:AHG88975.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        249..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          271..335
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          387..657
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   660 AA;  68167 MW;  36E85537C08383AE CRC64;
     MRRADERAAR RRLEQDAEFV AHLLAGRERS LAGGARVFAQ GPYFRGLVAS QRPLHDELLD
     QAMEAEDLLD ASWVFITDAR GRLLAKSDEP GAAGTDMGGV ALIAGALRGQ VMSGFGVSRD
     SLLFQVIAMP IAVPNGTPVG VLVATNVIGE EVVRDVRATT GSDVLFYALG VDGRPHIAAS
     SVARTTALDS ALGALSAGRR PGGGLLRVGA EDFHVQGARA TTAGGEAVGG WTVLRAHGAE
     ASEVAGMRAT VAAVAVVGLA LALLAAWLAA RQVTRPIRAL ATLAHRAVEG DYDPTRDGVE
     AVVGAADLDG EASDEIAALG AAFRAMIAEL RDREALTALG ARVPNEPAAA SAAVAAPTDA
     RGASAVSGVR VLRLASPARP ARLAERYELQ AVVGAGGTGI VYKALDDALG EIVAVKMLRP
     ELLAADPLAR ERLTHEIRLA RRISHRHVVR IHDIAENDGV PFLTMEFVDG PSLDALLHAR
     GALEPRAVLA VAKQLVRALD VAHTQGVVHG DLKPANLLVA PGGVVKVTDF GVARLVRGPV
     GPDAARIAGA VVGTPEYMAP ELLLGSAPDV RADIYAAGVV LHECLTGETP FNADTPVAFF
     AHKLDETPAR GTPIPQGPTL AAPRGIAAAL GALVAQMTAA DPAGRPASAR AVYAMLLRIG
//
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