PKNF_MYCTO
ID PKNF_MYCTO Reviewed; 476 AA.
AC P9WI74; L0T7T0; O08151; P72003;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Serine/threonine-protein kinase PknF;
DE EC=2.7.11.1;
GN Name=pknF; OrderedLocusNames=MT1788;
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 play a role in the regulation of glucose transport, cell
CC growth and septum formation. {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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Dephosphorylated by PstP (By similarity).
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; AE000516; AAK46061.1; -; Genomic_DNA.
DR PIR; C70986; C70986.
DR RefSeq; WP_003899000.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WI74; -.
DR SMR; P9WI74; -.
DR EnsemblBacteria; AAK46061; AAK46061; MT1788.
DR GeneID; 45425719; -.
DR KEGG; mtc:MT1788; -.
DR PATRIC; fig|83331.31.peg.1920; -.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Serine/threonine-protein kinase PknF"
FT /id="PRO_0000428056"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 332..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 8
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 287
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 290
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 476 AA; 50668 MW; 8A9C755F912D4776 CRC64;
MPLAEGSTFA GFTIVRQLGS GGMGEVYLAR HPRLPRQDAL KVLRADVSAD GEYRARFNRE
ADAAASLWHP HIVAVHDRGE FDGQLWIDMD FVDGTDTVSL LRDRYPNGMP GPEVTEIITA
VAEALDYAHE RRLLHRDVKP ANILIANPDS PDRRIMLADF GIAGWVDDPS GLTATNMTVG
TVSYAAPEQL MGNELDGRAD QYALAATAFH LLTGSPPFQH ANPAVVISQH LSASPPAIGD
RVPELTPLDP VFAKALAKQP KDRYQRCVDF ARALGHRLGG AGDPDDTRVS QPVAVAAPAK
RSLLRTAVIV PAVLAMLLVM AVAVAVREFQ RADDERAAQP ARTRTTTSAG TTTSVAPAST
TRPAPTTPTT TGAADTATAS PTAAVVAIGA LCFPLGSTGT TKTGATAYCS TLQGTNTTIW
SLTEDTVASP TVTATADPTE APLPIEQESP IRVCMQQTGQ TRRECREEIR RSNGWP
