ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P54741


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AFSK_STRCO
Primary accession number P54741
Secondary accession numbers Q9F365 Q9L002
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on August 14, 2001 (Sequence version 2)
Annotations were last modified on    October 14, 2008 (Entry version 69)
Name and origin of the protein
Protein name Serine/threonine-protein kinase afsK
Synonym EC 2.7.11.1
Gene name
Name: afsK
OrderedLocusNames: SCO4423
ORFNames: SC6F11.21, SCD6.01
From
Streptomyces coelicolor [TaxID: 1902] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Streptomycineae; Streptomycetaceae; Streptomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A3(2);
DOI=10.1016/0378-1119(94)90832-X; PubMed=8063104 [NCBI, ExPASy, EBI, Israel, Japan]
Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T.;
"Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase.";
Gene 146:47-56(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A3(2);
DOI=10.1016/0378-1119(95)00771-7; PubMed=8635757 [NCBI, ExPASy, EBI, Israel, Japan]
Ueda K., Umeyama T., Beppu T., Horinouchi S.;
"The aerial mycelium-defective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2).";
Gene 169:91-95(1996).
[3]
SEQUENCE REVISION TO 239-240.
Matsumoto A., Hong S., Ishizuka H., Horinouchi S., Beppu T., Umeyama T.;
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-471 / A3(2) / M145;
DOI=10.1038/417141a; PubMed=12000953 [NCBI, ExPASy, EBI, Israel, Japan]
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2).";
Nature 417:141-147(2002).
[5]
INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-44.
PubMed=11544211 [NCBI, ExPASy, EBI, Israel, Japan]
Umeyama T., Horinouchi S.;
"Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein.";
J. Bacteriol. 183:5506-5512(2001).
[6]
AUTPOPHOSPHORYLATION AT SER-71 AND THR-168, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-71; SER-128; THR-168 AND THR-170.
PubMed=16629414 [NCBI, ExPASy, EBI, Israel, Japan]
Tomono A., Mashiko M., Shimazu T., Inoue H., Nagasawa H., Yoshida M., Ohnishi Y., Horinouchi S.;
"Self-activation of serine/threonine kinase AfsK on autophosphorylation at threonine-168.";
J. Antibiot. 59:117-123(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D45382; BAA08229.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL939120; CAD55483.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_733637.1; -.
3D structure databases
HSSP P71584; 1O6Y. [HSSP ENTRY / PDB]
ModBase P54741.
Family and domain databases
InterPro IPR002372; PQQ_repeat.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR011047; Quino_AlcDHase-like.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Gene3D G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 2.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00564; PQQ; 9.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P54741.
ProtoNet P54741.
Genome annotation databases
GeneID 1099863; -.
GenomeReviews AL645882_GR; SCO4423.
KEGG sco:SCO4423; -.
NMPDR fig|100226.1.peg.4378; -.
Phylogenomic databases
HOGENOM P54741; -.
Other
LinkHub P54741; -.
Genome annotation databases
CMR P54741; SCO4423.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   799  799     Serine/threonine-protein kinase afsK. PRO_0000171234
DOMAIN   16   271  256     Protein kinase. 
NP_BIND   22    30  9     ATP (By similarity). 
COMPBIAS   317   428  112     Pro-rich. 
ACT_SITE   138   138        Proton acceptor (By similarity). 
BINDING   44    44        ATP (By similarity). 
MOD_RES   71    71        Phosphoserine; by autocatalysis. 
MOD_RES   168   168        Phosphothreonine; by autocatalysis. 
MUTAGEN   44    44        K->A: No autophosphosphorylation. Binds kbpA. 
MUTAGEN   71    71        S->A: No autophosphorylation. 
MUTAGEN   128   128        S->A: No change in autophosphorylation. 
MUTAGEN   168   168        T->A: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on afsR. Very little constitutive kinase activity. 
MUTAGEN   168   168        T->D: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on afsR. Constitutive kinase activity. 
MUTAGEN   168   168        T->E: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on afsR. Some constitutive kinase activity. 
MUTAGEN   170   170        T->D: No change in autophosphorylation. 
Sequence information
Length: 799 AA [This is the length of the unprocessed precursor] Molecular weight: 83788 Da [This is the MW of the unprocessed precursor] CRC64: 4BE9BED4169F6F5B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVDQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL AEDQLFRVRF 

        70         80         90        100        110        120 
TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL EEIVNECGPM PAQAVRWLAA 

       130        140        150        160        170        180 
GVAEALQSIH GAGLVHRDLK PSNVLVVEDG PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM 

       190        200        210        220        230        240 
SPEQAKDSRS VTGASDVFSL GSMLVFAATG HPPFHGANPV ETVFMLLREG PDLEGLPDEL 

       250        260        270        280        290        300 
RPLIESCMQM EATGRPNPAD LQAQLAPHLF GSGSDDSGTA SAWLPERAVG LIEGRRNGRP 

       310        320        330        340        350        360 
AVKPATTAGG RGHGHGPSGA RAPVHAPPLP PPPAHDPVVP APPAHVPAVP APVGAPDGGP 

       370        380        390        400        410        420 
VRLPGAAVPI GPGPRVADMR AAAVAAPPPE SALAASWSRP RPGVNGADPA VPAPAPAPPE 

       430        440        450        460        470        480 
ASPAGWRPWR FRMSNDVWGT PRVAEDLVYV TSFEVHALDV ATGRRRFKTR DVAWSMAVAD 

       490        500        510        520        530        540 
GRIHASDGPT LFALDAREGA DLWRVQTDAW VYSLQADRGT VLTATRGGGV QAWEASAGQK 

       550        560        570        580        590        600 
LWEVTGAQTD FESPEAGAAL HDGTAYVWQD ARLRALDART GDERWSYPIG DAASCGGVPV 

       610        620        630        640        650        660 
RLTQAPDGYV YVAAGTRVLA LEVASGHVRW HFEAPAVFLA PPTFVPGPAV TGGGVYLADY 

       670        680        690        700        710        720 
LGTVYALDAT DGRDRWRIAT EARSSTDPVL VAAGHVHVGS GKGLYTLDAV TGTPKWRFQA 

       730        740        750        760        770        780 
GGDIVGAPAV AEGRIHFGSS DHLLYTLKAD DGRLRWKLAT GGEITGSPVV RDGIVYACSK 

       790 
DRCVYALDAE KGTGTARTT 

P54741 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!