ID B2HLT3_MYCMM Unreviewed; 994 AA.
AC B2HLT3;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Serine/threonine-protein kinase transcriptional regulatory protein PknK_2 {ECO:0000313|EMBL:ACC38832.1};
GN Name=pknK_2 {ECO:0000313|EMBL:ACC38832.1};
GN OrderedLocusNames=MMAR_0365 {ECO:0000313|EMBL:ACC38832.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC38832.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC38832.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
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DR EMBL; CP000854; ACC38832.1; -; Genomic_DNA.
DR RefSeq; WP_012392346.1; NC_010612.1.
DR AlphaFoldDB; B2HLT3; -.
DR STRING; 216594.MMAR_0365; -.
DR KEGG; mmi:MMAR_0365; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3903; Bacteria.
DR HOGENOM; CLU_004665_5_3_11; -.
DR OrthoDB; 136365at2; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR47691:SF3; HTH-TYPE TRANSCRIPTIONAL REGULATOR RV0890C-RELATED; 1.
DR PANTHER; PTHR47691; REGULATOR-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ACC38832.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Transferase {ECO:0000313|EMBL:ACC38832.1}.
FT DOMAIN 14..271
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 994 AA; 107607 MW; AB9A6C5E0F926D68 CRC64;
MVSQLIGQLG ADGFADAVEV GRGGFGVVYR ARQVELDRVV AVKVLTADLE QNRPRFEREQ
RAMARLTGHP NIVSVLQVGH TPGGYPYLVM PFCSRGSVQE VITECGGLAV SEVLRLGVAV
AAGLESAHRL GIVHRDVKPA NVLLTEFGDP ALTDFGIAHM VGGFHTASGV FSATPDFTAP
EVLSGKEPDQ ASDVYGLGAT LFCALTGQPP FARRDGEVLM AQLLRIATES APDLRAYGVD
DDLAVVIGAA LAPEPTARPA MVEFGEALQE LQATRGLAID AMALQGAKHT GKTAAARPVP
PPRVRGNLPA PLSEFVGRAA ELAALAELFS TARLVTLVGV GGVGKTTLAL RAARTRAADY
PAGVWVIDIG ELRDGALLPG LAAGALGIHD QGSRALPEVM VDAIGEREML LVFDNCEHVI
DEAAALIDTL LRGCPRLQIV ATSRELLSLD GEAVFAVSPL RYPDTTTGTS RAALADYDAV
ALFVERAQAA RPGFTLTEHN AGAIALICSR LDGVPLAVEL AAARVRAMSV QQIAARLSES
FALLSRGYRG SPTHQQTLRC CIDWSYQRCS TAEQQLWARL SVFAGSFDLD LAHHVCAPDT
CPDDLLDQLC ELVDKSILSR IDNNDDAEVR FRLLATLREY GASCLTAADH QLLRQRHLDG
YRQLVAKAHA EWFSEHQVNW IRRMRRELPN VQEALQFGLT HAPDTALEMV ADLRMLFIVS
GKLKEGRRWL DRALSATPES STKNRIRGLT TGVGFAYFQM DWPAVTQWLA EARNLLELEP
YPEMDGLLCG YDGFSTLLRG EIDQARVSAE RGLAITGDYD DYQVRIGCMW VMSFHSALVG
DADQALHWAE RAYALAESRH EVQMRTFTVS ALVVGWLTRG DVEHADSALR KALELCRASD
YPFAGAQCLE GMAWTSAANN NLRRAVVLMT AAATISQITT GSSTTFFAVM GPFHADCERR
ARAELSETEF ESARIQGESL TFDEAVAFAL GHEW
//
