AFSK_STRGR
ID AFSK_STRGR Reviewed; 807 AA.
AC P54742;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Serine/threonine-protein kinase AfsK;
DE EC=2.7.11.1;
GN Name=afsK;
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8635757; DOI=10.1016/0378-1119(95)00771-7;
RA Ueda K., Umeyama T., Beppu T., Horinouchi S.;
RT "The aerial mycelium-defective phenotype of Streptomyces griseus resulting
RT from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor
RT A3(2).";
RL Gene 169:91-95(1996).
CC -!- FUNCTION: Component of the AfsK/AfsR system involved in the response of
CC aerial mycelium formation to glucose.
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 -!- SUBUNIT: Interacts (via the N-terminal kinase domain) with KbpA; the
CC interaction prevents autophosphorylation of AfsK. {ECO:0000250}.
CC -!- PTM: Autophosphorylated mainly on threonine residues. Some
CC phosphorylation on serine residues. Autophosphorylation on Thr-168 is
CC the major site enhancing kinase activity towards AfsR, and is regulated
CC though interaction with KbpA (By similarity). {ECO:0000250}.
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; D45246; BAA08203.1; -; Genomic_DNA.
DR AlphaFoldDB; P54742; -.
DR SMR; P54742; -.
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; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025666; PQQ-like_dom.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR Pfam; PF13570; PQQ_3; 1.
DR SMART; SM00564; PQQ; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50998; SSF50998; 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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..807
FT /note="Serine/threonine-protein kinase AfsK"
FT /id="PRO_0000171235"
FT DOMAIN 16..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 292..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Basic and acidic 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 MOD_RES 71
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 807 AA; 85232 MW; 66C274219155D091 CRC64;
MVEQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL AEDQLFRVRF
TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL EEIVNECGPM PTQAVRWLAA
GIAQALQSIH GAGLVHRDLK PSNVLVVEDG PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM
SPEQARDSRS VTGASDIFSL GSTLVFAATG HAPFHGANPV ETVFMLVREG PDLEGLPDDL
RPLIESCMQM DATHPAAEPR DLQAQLAPHL FASGSDDSGT ASAWLPVPAT AMIERRRGGR
RTARRPPRPR PRRLRAAPQG PGAGHRLAQR GRPAFALPAV LALAAVRRVR TAAGPSAAPD
GGPVQLPGAK VPIGPGRRAG EGRGAAAAAP RRRDRLGPAA RRSERFLGGH GPHRTVPAST
LRPGTPSPAP DRWRPWRFRM SNDVWGTPVV SGDLLYVTSF EVHALDVGNG RRQFKTRDVA
WAMAVEGGRI HASDGPSLYA LDAASGAEQW RLATDAWVYA LKADRGTVLT ATRGGGVQGW
EASNGEKLWE VTGAQSDFET AEAGPVIHDG TVYLWQDARL RALDARTGLE RWSYPIGDAA
SCGGVPVRVT PATDGYVYVA AGTRVLAVET GSGPVRWHFE APAVFLSPPA FAPGPAVTGG
GVYLADYLGT VYALDATTGK DRWRIATEAR SSIEPVLVAV GNVHVGSGSA LYTLDAVTDT
PKWRFAAGGD VVGAPWWRRP GPLRLGGPRA LHPGRGGRPA ALKLATGGEI TGSPVAQAGV
VYACSKDRCV YALDALKGTG TGNRART
