ID   A0A2K9LHN2_9GAMM        Unreviewed;       613 AA.
AC   A0A2K9LHN2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=Kalk_04215 {ECO:0000313|EMBL:AUM11671.1};
OS   Ketobacter alkanivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Ketobacteraceae; Ketobacter.
OX   NCBI_TaxID=1917421 {ECO:0000313|EMBL:AUM11671.1, ECO:0000313|Proteomes:UP000235116};
RN   [1] {ECO:0000313|Proteomes:UP000235116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GI5 {ECO:0000313|Proteomes:UP000235116};
RA   Kim S.-J., Rhee S.-K.;
RT   "Direct submision.";
RL   Submitted (AUG-2017) 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; CP022684; AUM11671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K9LHN2; -.
DR   KEGG; kak:Kalk_04215; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000235116; 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-EC.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235116};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        531..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..254
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          278..576
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          575..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  68509 MW;  DED1AAC61E059519 CRC64;
     MELEGFSQLE KIAEGGMAVL YRGIQSSLSR PVAIKVMKGA LSGTPEAHEM FEAESRIVAR
     LDHPHIIRVI DRGLTADEMP YFVMDYVEGL TLKDALKTQK LSDRRKLRII MQIAKALGYA
     HKNNVIHRDI KPGNILLDKE GNARVVDFGI ARLSEDTEVS IREESMTVGT PAYMAPEQRR
     GAAFTSSASD IYSLGVIMYL MLASKLPKAG YPAPSHFNPK IPSSLDKITM ACLADDPDRR
     PSADKLVALL LKALKGAHLK QEQKAQAQDT FKDPKEKFRL LDVIRETPYG TVCLYENRED
     HSLMVLKKRV GNFQGYNESE ILSRVKHRNI INVRGVSRND RIFITILEYL SGGSLQNRMA
     QPMPPTTFTA VADQICDAMI FAHNNRIVHG NLRPHNILFD DTNTVKVMDF GFEPHYAEAA
     EQNWYKAPGE TASVLADIFA AGVIFYQLLT GMLPEWKRGL LQPCEPFATI PQHLRTLIKG
     MLCLEAHVRI QSFEEVKRCL HLIEEDEDEK TRTKIKQHAP SKKRRSPLRS LAMVLALLLL
     VGVNGALYSW LLLKKGQDMP AVASILASLG FEHPTATPTP ESASQTASSI PPKTASKPDQ
     ELTLRRVDQA KQN
//