PKNH_MYCTO
ID PKNH_MYCTO Reviewed; 626 AA.
AC P9WI70; L0T6C9; Q11053;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Serine/threonine-protein kinase PknH;
DE EC=2.7.11.1;
GN Name=pknH; OrderedLocusNames=MT1304;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: May regulate bacterial growth in response to external signals
CC to facilitate adaptation to the host environment. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on threonine and serine residues.
CC Dephosphorylated by PstP (By similarity). {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; AE000516; AAK45563.1; -; Genomic_DNA.
DR PIR; B70754; B70754.
DR RefSeq; WP_003898799.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI70; -.
DR SMR; P9WI70; -.
DR EnsemblBacteria; AAK45563; AAK45563; MT1304.
DR KEGG; mtc:MT1304; -.
DR PATRIC; fig|83331.31.peg.1409; -.
DR HOGENOM; CLU_000288_63_44_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.1000.70; -; 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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14032; PknH_C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Disulfide bond; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..626
FT /note="Serine/threonine-protein kinase PknH"
FT /id="PRO_0000428058"
FT TOPO_DOM 1..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..626
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..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
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:0000305"
FT DISULFID 482..545
FT /evidence="ECO:0000250"
FT DISULFID 587..604
FT /evidence="ECO:0000250"
SQ SEQUENCE 626 AA; 66726 MW; 927C5D0835F05757 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 SQESTLPAPP
KPVPPPTMPA TAMAPRQPPA PPVTPPGVQP APKPSYTPPA QPGPAGQRPG PTGQPSWAPN
SGPMPASGPT PTPQYYQGGG WGAPPSGGPS PWAQTPRKTN PWPLVAGAAA VVLVLVLGAI
GIWIAIRPKP VQPPQPVAEE RLSALLLNSS EVNAVMGSSS MQPGKPITSM DSSPVTVSLP
DCQGALYTSQ DPVYAGTGYT AINGLISSEP GDNYEHWVNQ AVVAFPTADK ARAFVQTSAD
KWKNCAGKTV TVTNKAKTYR WTFADVKGSP PTITVIDTQE GAEGWECQRA MSVANNVVVD
VNACGYQITN QAGQIAAKIV DKVNKE
