ID   A0JV78_ARTS2            Unreviewed;       710 AA.
AC   A0JV78;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Arth_1554 {ECO:0000313|EMBL:ABK02948.1};
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK02948.1, 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};
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DR   EMBL; CP000454; ABK02948.1; -; Genomic_DNA.
DR   RefSeq; WP_011691414.1; NC_008541.1.
DR   AlphaFoldDB; A0JV78; -.
DR   STRING; 290399.Arth_1554; -.
DR   KEGG; art:Arth_1554; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_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:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 4.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABK02948.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000754};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABK02948.1};
KW   Transferase {ECO:0000313|EMBL:ABK02948.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        420..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          446..511
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          512..579
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          580..647
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          648..710
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          659..697
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          300..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  75032 MW;  4473E749F2E70805 CRC64;
     MQDKVSDPLV GTLVDNRYRV QSRLARGGMS TVYLATDQRL ERDVALKVLH PHLVNDGNFL
     DRLGREAKAA AKLSHAHVVG VLDQGSDGHT AYLVMEYIKG HTLRDVIKEK GALSPRLALA
     LIDPVVEGLG AAHAAGLIHR DIKPENVLIA DDGRIKVGDF GLARAVTTST STGALIGTVA
     YLSPELVLGR QADARSDIYS VGIMLYEMIT GSQPFDGDVP IQVAYQHVNS SVEAPSAVVP
     GLAAEVDELV QWCTARDPEQ RPVDGNALLS ELRHIRTNLT DAELDLQPPA AIAAVAHAPS
     ELRPPAHPPT SRPSEARSPA RQDQTEILSA GQHPTEIINR QSNPTTVLSA GRRPGQFGAL
     AAPAEPEPAF GDPGDDGPDT AVPLSKRAQR KLDREAARAE SKAASTPVRS LREGNPRRRG
     LLWIIILVIA ALLATGAGWF FGMGPGSPGT IPRVANKTVA EAQQLLGTAG FQSTTKDVFD
     DDIRAGLVVG TEPEAGREIR KFQMVSLFVS KGPQLFPLPG VSGKSLDEAK NQLNSAEMAL
     GTVTETYSET EPAGTILAQD PAAGTPARRG TPVSLTVSKG PEPIPVPDMR GQEQGAAVKA
     LEAAGLKAVI SPETVNDKKV PKGAVVAQEP SNGTLTRGAT VTLTVSKGPK LVNVPSYIGK
     QANDARKALE KLGFEVRVNN ILGGFFGTVR DQDPVDTQVP EGSVVTLTVV
//