ID E6J6P0_9ACTN Unreviewed; 826 AA.
AC E6J6P0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Serine/threonine protein kinase PknG {ECO:0000313|EMBL:EFV92735.1};
GN ORFNames=ES5_04403 {ECO:0000313|EMBL:EFV92735.1};
OS Dietzia cinnamea P4.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV92735.1, ECO:0000313|Proteomes:UP000004165};
RN [1] {ECO:0000313|EMBL:EFV92735.1, ECO:0000313|Proteomes:UP000004165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4 {ECO:0000313|EMBL:EFV92735.1,
RC ECO:0000313|Proteomes:UP000004165};
RX PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L., Sorensen S.J.,
RA Cardoso J.S., Padula M., Leitao A.C., Seldin L., van Elsas J.D.;
RT "Insight from the draft genome of Dietzia cinnamea P4 reveals mechanisms of
RT survival in complex tropical soil habitats and biotechnology potential.";
RL Antonie Van Leeuwenhoek 101:289-302(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:EFV92735.1}.
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DR EMBL; AEKG01000099; EFV92735.1; -; Genomic_DNA.
DR RefSeq; WP_007627865.1; NZ_AEKG01000099.1.
DR AlphaFoldDB; E6J6P0; -.
DR Proteomes; UP000004165; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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:EFV92735.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:EFV92735.1}; Transferase {ECO:0000313|EMBL:EFV92735.1}.
FT DOMAIN 210..477
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 89226 MW; 00300F1C7EA71864 CRC64;
MSYRKWDDPP EDGEPTVGTQ ATVRTEAVAV TQAAAATGAM AETGAAAATG ATEATGAMEA
TGAMAETGGS ASTGGMAETG AVDATGAVSM TGFLSDTDPD AGTTPRAAGR PGHDPESRTE
SVPGARPSGR TDSVTGDRAT SAPFRMRHPD KPEDRPSQAA EGLVDLPYII PVDPTSAMLA
PEDIEAECAA SNGKLPRPEL RPGDIVADQY EVRGALAHGG MGWIYLAVDH NVSDRWVVLK
GLLHADQAEA QEVAVAEREI LAELSHPSIV RIYNFIHDDW ATSPTHGGYI VMEYVGGPSL
RDVRRAAPGR VLPVEKAIAY VLEVLQALSY LHSVGLVYND LKPENIMLTE DHVKLIDMGA
VSGVGDYGHI YGTPGFQAPE IPETGPTIVS DLYTVGRTLA SLIVRLPVVD GRYADGIPSP
MEEPVFSRYD SLYRFLLRST HEDPDMRFRS ATGMANQLMG VLREVLALRT GVPHPAFSSV
FSPQRSTFGT LFTVEPTDFL VDGRARDTTL TGAELVDALP VPLMESSDPA SRILAATSYT
SVEQRIDTLK ELYSDTESEA HESIGVIMSL ARAYLESGDL AAAEALLEEN AHRRRAEWRL
VWYDGIVALL KGDPVGAYPK FQQVLSAMPG ENGPKLALAA TAELILDVCP ERDRARWARS
SEHFYRTVWS VDRSVISSAF GLARQLQRRG EVAAAIEELD RVPPNSRYSS LANLTAILLL
CQGRPLEETE ESHLREAARR VTNLSAGEHR AFQIRLTVLT TALAWIQLPG NEPSPSPLMR
GVPFTEFGLR SGAETVLRTL ARSTETRAQR FRLVDQANSI RPRTLF
//