ID K5BKU2_MYCHD Unreviewed; 755 AA.
AC K5BKU2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknG {ECO:0000313|EMBL:VCT92985.1};
GN ORFNames=C731_0572 {ECO:0000313|EMBL:EKF25459.1}, MHAS_04723
GN {ECO:0000313|EMBL:VCT92985.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF25459.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF25459.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF25459.1}, and DSM 44199 / CIP
RC 105218 / JCM 12690 / 3849 {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2] {ECO:0000313|EMBL:VCT92985.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT92985.1};
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000268660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000268660};
RX PubMed=30701245; DOI=10.1128/mra.01522-18;
RA Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL Microbiol. Resour. Announc. 8:e01522-e01522(2019).
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};
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DR EMBL; AMRA01000015; EKF25459.1; -; Genomic_DNA.
DR EMBL; LR026975; VCT92985.1; -; Genomic_DNA.
DR RefSeq; WP_005624351.1; NZ_LR026975.1.
DR AlphaFoldDB; K5BKU2; -.
DR STRING; 1122247.GCA_000379865_02016; -.
DR KEGG; mhas:MHAS_04723; -.
DR PATRIC; fig|1122247.3.peg.548; -.
DR eggNOG; COG0515; Bacteria.
DR OMA; PHCGSAY; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR Proteomes; UP000268660; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031634; PknG_rubred.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16919; PknG_rubred; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EKF25459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VCT92985.1}.
FT DOMAIN 157..428
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 81937 MW; 10813EE7DD878DAA CRC64;
MSETRSDGFD DAGPGTQPAS LDDLFLDSAS TARPMATQAV YRPRFDDDDE GSRAATAGTD
SRDQATATTA VTRLSPTRRL GGGLVEIPRV PAKDPLEALM PDPEVAENKR FCWNCGRPVG
RSSKDGPARP EGFCPHCGSQ YSFLPQLNPG DMVADQYEIK GCIAHGGLGW VYLAFDHNVN
KRPVVLKGLV HSGDAEAQKI AMAERRFLAE VTHPGIVKIY NFVEHDDKHG NPVGYIVMEY
VGGTSLKQAK AKKLPVAQAI GYMLEILPAL GYLHSIGLAY NDLKPENIMI TEEQLKLIDL
GAVSTINSFG YLYGTPGYQA PEIVRTGPTV QTDIYTVGRT LAALTLNLPT RKGRYVDGLP
EDDPVLAEYD SYARLLRRAT DPDPRRRFSS AEEMSSQLLG VLREVVAKDT GVPRPGLSTV
FSPTRSTFGI DLLVAHTDVY LDGQVHSERL TAQEIVRALP VPLVDPTDVG APVLSASVLS
QPVQTLDQLR AARHGALDSE GIDLSQSVEL PLMEARALLD LGDVAKATRK LNDLAERVGW
TWRLLWFRGV ADLLTADYDS AERHFTQVLD TLPGELAPKL ALAATLELAG KDPGKFYNTV
WSTDNGIISA GFGLARAQSA AGDRDAAVRT LDKVPAMSRH YTTARLTSAV TLLSGRSTSE
ITEEHIREAA RRVEALPDTE PRVLQIRALV LGTAMDWLAD HTASTNHILG FPFTEHGLQL
GVEASLRALA RVAPSQAHRY ALVDLANSVR PTTTF
//