ID   PKNH_MYCBO              Reviewed;         596 AA.
AC   Q7U095; A0A1R3XXU3; X2BH99;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Serine/threonine-protein kinase PknH;
DE            EC=2.7.11.1;
GN   Name=pknH; OrderedLocusNames=BQ2027_MB1297C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated on threonine and serine residues.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; LT708304; SIT99898.1; -; Genomic_DNA.
DR   RefSeq; NP_854951.1; NC_002945.3.
DR   RefSeq; WP_010950514.1; NC_002945.4.
DR   AlphaFoldDB; Q7U095; -.
DR   SMR; Q7U095; -.
DR   PATRIC; fig|233413.5.peg.1422; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.1000.70; PknH-like extracellular domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR026954; PknH-like_Extracell.
DR   InterPro; IPR038232; PknH-like_Extracell_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF14032; PknH_C; 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; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..596
FT                   /note="Serine/threonine-protein kinase PknH"
FT                   /id="PRO_0000171217"
FT   TOPO_DOM        1..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..596
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          16..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          292..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..322
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         22..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         170
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   596 AA;  63697 MW;  5E335EF65DD53D97 CRC64;
     MSDAQDSRVG SMFGPYHLKR LLGRGGMGEV YEAEHTVKEW TVAVKLMTAE FSKDPVFRER
     MKREARIAGR LQEPHVVPIH DYGEVDGQMF LEMRLVEGTD LDSVLKRFGP LTPPRAVAII
     TQIASALDAA HADGVMHRDV KPQNILITRD DFAYLVDFGI ASATTDEKLT QLGTAVGTWK
     YMAPERFSND EVTYRADIYA LACVLHECLT GAPPYRADSA GTLVSSHLMG PIPQPSAIRP
     GIPKAFDAVV ARGMAKKPED RYASAGDLAL AAHEALSDPD QDHAADILRR SQESTLPGTA
     AVTAQPPTMP TVTPPPIQAA PTGQPSWAPN SGPMPASGPT PTPQYYQGGG WGAPPSGGPS
     PWAQTPRKTN PWPLVAGAAA VVLVLVLGAI GIWIANRPKP VQPPQPVAEE RLSALLLNSS
     EVNAVMGSSS MQPGKPITSM DSSPVTVSLP DCQGALYTSQ DPVYAGTGYT AINGLISSEP
     GDNYEHWVNQ AVVAFPTADK ARAFVQTSAD KWKNCAGKTV TVTNKAKTYR WTFADVKGSP
     PTITVIDTQE GAEGWECQRA MSVANNVVVD VNACGYQITN QAGQIAAKIV DKVNKE
//