ID   A0JUG8_ARTS2            Unreviewed;       581 AA.
AC   A0JUG8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABK02688.1};
GN   OrderedLocusNames=Arth_1294 {ECO:0000313|EMBL:ABK02688.1};
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK02688.1, ECO:0000313|Proteomes:UP000000754};
RN   [1] {ECO:0000313|Proteomes:UP000000754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
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 protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP000454; ABK02688.1; -; Genomic_DNA.
DR   RefSeq; WP_011691155.1; NC_008541.1.
DR   AlphaFoldDB; A0JUG8; -.
DR   STRING; 290399.Arth_1294; -.
DR   KEGG; art:Arth_1294; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_129_0_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000000754; 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-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABK02688.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000754};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABK02688.1};
KW   Transferase {ECO:0000313|EMBL:ABK02688.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          339..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..355
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   581 AA;  61816 MW;  431C6D96CA365CBA CRC64;
     MSAKRPVAPP PAIPGFTYVS LLGSGGFSDV YLYEQDRPRR KVAVKVLLSD LKTEGARRRF
     ESEANLMAQL SSHPYIVTIF EAEVTEDGHS YLAMEYCSRP SLDVRYRRQR FSVDEVLAVG
     IQVASAVETA HRAGIAHRDI KPANILVTDY NRPALTDFGI SGTLGSDTDE DAGMSIPWSP
     PEQFRDGPVD GVMVDVWALG ATLYTLLAGR SPFVLPGADN SQRELISRIT NSPVPRLGRA
     DVPESLELAL ATAMAKSAAS RYSSAHAFAL ALQRIQAELN LSVTPFEVLE EAHGEENHPD
     DGFEETRVRS IASVDPDQTG NAPTFPARTR PAAFTPVVPV APPAGPAPGP VPGPGARPDL
     HDDWSQGTML RGSVASGLQP GGGHDAADDA TVHRGAPGRP AGWQGGPAGR DDRGDEHVAA
     TVNRPQALQE ATAEGPVDHS KRNLWLSVAG GAVLVVAVVV GLVLGASRPE PVVEPTGQVS
     KPPADAIGDG TVPDVTNIKA VTEAGKVRFT WTNPQPKPGD TYKWQLTNYG QEEGPFQSSK
     EAQAEVAYGK ADFFCIKVMI VRSDGSASPM TSRDAYSCMP S
//