PKWA_THECU
ID PKWA_THECU Reviewed; 742 AA.
AC P49695;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable serine/threonine-protein kinase PkwA;
DE EC=2.7.11.1;
GN Name=pkwA; Synonyms=pkw1;
OS Thermomonospora curvata.
OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC Thermomonospora.
OX NCBI_TaxID=2020;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCM 3352;
RX PubMed=8631732; DOI=10.1128/jb.178.5.1487-1489.1996;
RA Janda L., Tichy P., Spizek J., Petricek M.;
RT "A deduced Thermomonospora curvata protein containing serine/threonine
RT protein kinase and WD-repeat domains.";
RL J. Bacteriol. 178:1487-1489(1996).
CC -!- FUNCTION: May play a regulatory role during the complex growth cycle
CC and in secondary metabolite production.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF115313; AAB05822.1; -; Genomic_DNA.
DR PDB; 5YZV; X-ray; 2.60 A; A/B/C/D/E=441-742.
DR PDBsum; 5YZV; -.
DR AlphaFoldDB; P49695; -.
DR SMR; P49695; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..742
FT /note="Probable serine/threonine-protein kinase PkwA"
FT /id="PRO_0000171245"
FT DOMAIN 16..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 455..496
FT /note="WD 1"
FT REPEAT 497..538
FT /note="WD 2"
FT REPEAT 539..580
FT /note="WD 3"
FT REPEAT 581..621
FT /note="WD 4"
FT REPEAT 622..663
FT /note="WD 5"
FT REPEAT 664..705
FT /note="WD 6"
FT REPEAT 706..742
FT /note="WD 7"
FT REGION 266..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 471..478
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 483..491
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:5YZV"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 555..562
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:5YZV"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 588..593
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 597..604
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:5YZV"
FT TURN 614..617
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 618..623
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 630..635
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 639..648
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:5YZV"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 671..676
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 680..687
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:5YZV"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 715..718
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 725..728
FT /evidence="ECO:0007829|PDB:5YZV"
FT STRAND 732..737
FT /evidence="ECO:0007829|PDB:5YZV"
SQ SEQUENCE 742 AA; 78950 MW; AC1734640DB4383D CRC64;
MIEPLQPGDP GRIGPYRLVS RLGAGGMGQV FLARSPGGRP VVVKVILPEY ANDDEYRIRF
AREVEAARRV GGFHTAQVID ADPTADPPWM ATAYIPGPSL RKAVTERGPL YGNNLRTLAA
GLVEGLAAIH ACGLVHRDFK PSNIVLAADG PRVIDFGVAR PLDSSVMTQS GAVIGTLAYM
SPEQTDGSQV GPASDVFSLG TVLAFAATGR SPFMADSIGE IIARISGPPP ELPELPDDLR
ELVYACWEQN PDLRPTTAEL LAQLSTDHTG DDWPPPHLSD LIGSMLPLGA TTSPNPSLAI
EPPPPSHGPP RPSEPLPDPG DDADEPSAEK PSRTLPEPEP PELEEKPIQV IHEPERPAPT
PPRPREPARG AIKPKNPRPA APQPPWSPPR VQPPRWKQLI TKKPVAGILT AVATAGLVVS
FLVWQWTLPE TPLRPDSSTA PSESADPHEL NEPRILTTDR EAVAVAFSPG GSLLAGGSGD
KLIHVWDVAS GDELHTLEGH TDWVRAVAFS PDGALLASGS DDATVRLWDV AAAEERAVFE
GHTHYVLDIA FSPDGSMVAS GSRDGTARLW NVATGTEHAV LKGHTDYVYA VAFSPDGSMV
ASGSRDGTIR LWDVATGKER DVLQAPAENV VSLAFSPDGS MLVHGSDSTV HLWDVASGEA
LHTFEGHTDW VRAVAFSPDG ALLASGSDDR TIRLWDVAAQ EEHTTLEGHT EPVHSVAFHP
EGTTLASASE DGTIRIWPIA TE
