ID K0V0C3_MYCFO Unreviewed; 623 AA.
AC K0V0C3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Serine/threonine-protein kinase PknB {ECO:0000256|ARBA:ARBA00014672};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=MFORT_16719 {ECO:0000313|EMBL:EJZ12837.1};
OS Mycolicibacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 = JCM
OS 6387.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1214102 {ECO:0000313|EMBL:EJZ12837.1, ECO:0000313|Proteomes:UP000006043};
RN [1] {ECO:0000313|EMBL:EJZ12837.1, ECO:0000313|Proteomes:UP000006043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM46621 {ECO:0000313|Proteomes:UP000006043};
RX PubMed=23105073; DOI=10.1128/JB.01461-12;
RA Ho Y.S., Adroub S.A., Aleisa F., Mahmood H., Othoum G., Rashid F.,
RA Zaher M., Ali S., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium fortuitum subsp. fortuitum Type
RT Strain DSM46621.";
RL J. Bacteriol. 194:6337-6338(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJZ12837.1}.
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DR EMBL; ALQB01000067; EJZ12837.1; -; Genomic_DNA.
DR RefSeq; WP_003883288.1; NZ_JH814738.1.
DR AlphaFoldDB; K0V0C3; -.
DR GeneID; 83872819; -.
DR PATRIC; fig|1214102.3.peg.3317; -.
DR HOGENOM; CLU_000288_135_2_11; -.
DR Proteomes; UP000006043; Unassembled WGS sequence.
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 GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd06577; PASTA_pknB; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
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:EJZ12837.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:EJZ12837.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 329..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 353..419
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 420..487
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 488..553
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 554..623
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 433..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 623 AA; 66381 MW; 7D70CC9A701E46F8 CRC64;
MTTPQHLSDR YELGEILGFG GMSEVHLARD TRLHRDVAVK VLRADLARDP SFYLRFRREA
QNAAALNHPA IVAVYDTGEA ETPNGPLPYI VMEYVDGVTL RDIVHGEGPI PPRRAIEIIA
DACQALNFSH QHGIVHRDVK PANIMISKNN AVKVMDFGIA RALADTGNSV TQTAAVIGTA
QYLSPEQARG ETVDARSDVY SLGCVLYEIL TGEPPFIGDS PVAVAYQHVR EDPIPPSHRH
TGISPELDAV VLKALAKNPD NRYQTAAEMR TDLIRVHSGE APEAPKVLTD AERTSMMNSG
PMLAQGGGAP TQNLVVPRPA GRNASVARWL IAVAVLAVLT VVVTVAINMF DGKPRDVQVP
DVSGQRSADA VAALQNRGFK TRTEPKPDNQ VRPEYVISTD PAANSMAAAG DEITVNVSTG
PQQAQIPDVA GLSPSQARQK LKDAGFEKVK ESASPSTPEQ KGRVLATNPP ANQTAGIIYE
VTLVIGSGPE DTAVPDCKSQ SADVCKQILA ASGFTNTVVI DVDHTAPTGQ VVDTEPTSGT
SVPKDTPIQI HVSKGNQFVM PNLVGQFWDD AYQRLSALGW TGILDKGPDV RDSGQRTNAV
VTQSPPAGTG VNFGSKITLS FAS
//
