ID A0A1Y2MU90_PSEAH Unreviewed; 659 AA.
AC A0A1Y2MU90;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_1 {ECO:0000313|EMBL:OSY38711.1};
GN ORFNames=BG845_03913 {ECO:0000313|EMBL:OSY38711.1};
OS Pseudonocardia autotrophica (Amycolata autotrophica) (Nocardia
OS autotrophica).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=2074 {ECO:0000313|EMBL:OSY38711.1, ECO:0000313|Proteomes:UP000194360};
RN [1] {ECO:0000313|EMBL:OSY38711.1, ECO:0000313|Proteomes:UP000194360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 535 {ECO:0000313|EMBL:OSY38711.1,
RC ECO:0000313|Proteomes:UP000194360};
RA Grumaz C., Vainshtein Y., Kirstahler P., Sohn K.;
RT "Pseudonocardia autotrophica DSM535, a candidate organism with high
RT potential of specific P450 cytochromes.";
RL Submitted (SEP-2016) 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:OSY38711.1}.
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DR EMBL; MIGB01000021; OSY38711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2MU90; -.
DR STRING; 2074.BG845_03913; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000194360; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 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:OSY38711.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000194360};
KW Transferase {ECO:0000313|EMBL:OSY38711.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 366..432
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 433..501
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 502..568
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 569..635
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 462..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..635
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 659 AA; 69429 MW; DC2981FF7E00C668 CRC64;
MTTPRLLSER YELGDPLGYG GMSEVHRGLD TRLGRDVAVK VLRADLARDP QFQLRFRREA
QNSASLNHPA IVAVYDTGEI QSEFGPLPYI VMEFVDGQTL REIVKTTGPM TQQRVVEVMA
DVCAALDFSH RHNIIHRDVK PANVMINGVG AVKVMDFGIA RALGEGQNVT QTAAVIGTAQ
YLSPEQARGE AVDARSDVYA AGCVLFELLT GEPPFTGDTP VAVAYQHVRE DPRSPSELNP
SVPPALDAVV LKALSKNPAN RYQSAAEMRA DLVRVRNGEP VHAPLVMSEY ERTQMMAHDD
ATAAMATRRL DGGGGPPTGR HVMPGDYDYD DEQRPGRGRK IALWVAVLAV LGLLGFVGYQ
MFSSSAPDQV AVPDVLGQTP DQARATITNA GLLFTQENQP SDVAQVGQVV RTDPGGGNQV
PENSRVTVFV GTGPAEVTVP SLAGSTPEQA EAQLREAGLQ IGGRTEQDTS DSSQVGRVIS
SDPGPGQRVP GNSSVSLVIG REQQTIAVPD VSGSSAEEAR SALRNAGFTS IESSEVDGGG
TAGSVVGSDP SAGTRVARDQ TITIQVSRGN QTQIPNVVGQ RVDNAVNTLR EAGLSFSIQT
TDVSDPSQNG VVLSQDPTGG SQASDGRQVT LTVGRASGGD TGGDSGGDTG ESSRGFPFD
//
