ID A0A429DZF6_9ACTN Unreviewed; 676 AA.
AC A0A429DZF6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknB {ECO:0000313|EMBL:RSN42376.1};
GN ORFNames=DMH08_38665 {ECO:0000313|EMBL:RSN42376.1};
OS Actinomadura sp. WAC 06369.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2203193 {ECO:0000313|EMBL:RSN42376.1, ECO:0000313|Proteomes:UP000288610};
RN [1] {ECO:0000313|EMBL:RSN42376.1, ECO:0000313|Proteomes:UP000288610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 06369 {ECO:0000313|EMBL:RSN42376.1,
RC ECO:0000313|Proteomes:UP000288610};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RSN42376.1}.
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DR EMBL; QHJN01000301; RSN42376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429DZF6; -.
DR Proteomes; UP000288610; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RSN42376.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000288610};
KW Transferase {ECO:0000313|EMBL:RSN42376.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..281
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 465..532
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 533..596
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 615..676
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 282..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 70139 MW; 147B91E7F102D6E8 CRC64;
MDTTVADPLV GQLLDGRYRI ESRIARGGMA TVYLARDSRL DRVVAVKVMH AGLAADEDFV
NRFIGEAKAA AALSHPNVVA VYDQGTDGER GYLVMEYVPG RTLRDALAAR GRFGPRAALE
TMQPVLAALG AAHRAGLVHR DVKPENVLIT EDGQVKVTDF GLARAESASR MTRTGVIIGT
VGYLAPEQVT SGSADVRSDV YAAGIMLFEL LTGRLPHEGD TPLAVAYKHV NETVPPPSEL
VPGLPYRVDE LVTAATSRDP AHRPQDANAC LAAVAEVHGG LPPDIDARLE EAPPGGTAVL
PAPAGAAPPD GAADGGPAGH GGTEPLPPAP RTSPVRFPED VRGHTAVLDP GEDPAGPPPR
SRGDRVIGAL TGRYVLVAIG AIAAVILGWA VWYQTSGQYE HVPADIVGME VAEARGALAD
AGIAVRVAEP VYHDRVRKGL VAKSDPGAGA RVGQGETVTL TPSKGLTPRA VPDVEGKTLD
EAKKILADDG FRVGGTSTRE SQTVPKDRVV GTDPAAGKEL SPDEPVAVVL SGGMSMPDLV
GSNGETAANR LRSLGLKVTV REKRVEGKAP GTVVEQTPGE GTGVSRGDEV ALVVNERDCI
IDAGPIRLGC DGEGGAEKIP VPDVTHRSVD DATKILKDSG FEVNVQGWGG DTVRFQAPGG
DGTADRGSTV TIVRGP
//
