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Database: UniProt
Entry: A0A144P363_9GAMM
LinkDB: A0A144P363_9GAMM
Original site: A0A144P363_9GAMM 
ID   A0A144P363_9GAMM        Unreviewed;       713 AA.
AC   A0A144P363;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AMT96818.1};
GN   ORFNames=A3K91_1212 {ECO:0000313|EMBL:AMT96818.1};
OS   Psychrobacter alimentarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=261164 {ECO:0000313|EMBL:AMT96818.1, ECO:0000313|Proteomes:UP000076104};
RN   [1] {ECO:0000313|EMBL:AMT96818.1, ECO:0000313|Proteomes:UP000076104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27889 {ECO:0000313|EMBL:AMT96818.1,
RC   ECO:0000313|Proteomes:UP000076104};
RA   Lee J., Kim O.-S.;
RT   "Genome sequencing of Psychrobacter alimentarius PAMC 27889.";
RL   Submitted (MAR-2016) 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};
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DR   EMBL; CP014945; AMT96818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A144P363; -.
DR   STRING; 261164.A3K91_1212; -.
DR   KEGG; pali:A3K91_1212; -.
DR   PATRIC; fig|261164.3.peg.1279; -.
DR   Proteomes; UP000076104; 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; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AMT96818.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AMT96818.1};
KW   Transferase {ECO:0000313|EMBL:AMT96818.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        691..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..330
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          384..691
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  78898 MW;  B2163FA8BC3A39C4 CRC64;
     MLKAKRNANQ KSHQHRAHIS AKQATTEASA AMSTGGELSH PREDMALWWL DFFTTKGRKA
     ENQDSLLITT CLLPRLSPLA LSEQSLSTQP TMLPSSLSKA PLLVIMADGV SACQFPKQAS
     QLVVNTVAEK ITLALSKLAS VSPERQHSAQ TMSVDFDDDQ LAGIIKMAVN KANDMLYFPQ
     TYQRVPPLLS TLSGLLCIGD RIHLFHTGDS RIYRIGPDSL TVLSDDHRIH RGQDKGALSA
     AIGADGQLDL QQSVFTLHQN ECLAIMTDGV YEHIDEVELA FELCTAATQM GQTLSKTSSS
     PADFCVSQTV CEQAFAEGSH DNLSMIMLSM NAMPTLSKCI KNRADIDNHI EKLDTPINPD
     AVIHDSHHYQ LPPVLDIGDS IDGFTVMSII ARTARSQVYW VKDESDHDFV LKSPSLDTIE
     DGHYLRDFLQ ERKIGLSLSK HRRAGESAYN QSDPNHLPIT ESNKANAHVI GSGLNVSGLL
     RYYPVPASTT YLYHLTEYIE GESLRDFINS HAPCDVWQTY DLLTKIGMAA RVMHRNYLLH
     QDIKPENVLL TKSGAIKLID FGSASSSILK DSTRPPNGDL HYAAPEYYTN APKGVHSDLF
     SIAVIGYELL TGQLPFGSQE LMNPQQALVM PTKPLRQHNV PATSQQALIR ALHPNTKVRY
     QAIGEFLQDF NPDNSTRSRD SEPLIKSNPL LVWHGICFVQ TVIIVLLLWA YLS
//
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