ID   HASP_STRCO              Reviewed;         300 AA.
AC   Q9Z4Z7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=3-hydroxyasparagine phosphotransferase;
DE            EC=2.7.1.-;
DE   AltName: Full=CDA 3-hydroxyasparaginyl phosphotransferase;
GN   Name=hasP; OrderedLocusNames=SCO3234; ORFNames=SCE29.03;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND ROLE IN CDA BIOSYNTHESIS.
RC   STRAIN=A3(2) / 2377;
RX   PubMed=17322197; DOI=10.1099/mic.0.2006/002725-0;
RA   Neary J.M., Powell A., Gordon L., Milne C., Flett F., Wilkinson B.,
RA   Smith C.P., Micklefield J.;
RT   "An asparagine oxygenase (AsnO) and a 3-hydroxyasparaginyl
RT   phosphotransferase (HasP) are involved in the biosynthesis of calcium-
RT   dependent lipopeptide antibiotics.";
RL   Microbiology 153:768-776(2007).
CC   -!- FUNCTION: Phosphotransferase that is responsible for the production of
CC       the 3-phosphohydroxyasparaginyl residues found at position 9 in the
CC       non-ribosomally synthesized calcium-dependent antibiotic (CDA)
CC       derivatives CDA1b and CDA2a/b. It is not known whether the
CC       phosphorylation reaction takes place before, during or after peptide
CC       assembly. {ECO:0000269|PubMed:17322197}.
CC   -!- PATHWAY: Antibiotic biosynthesis; calcium-dependent antibiotic
CC       biosynthesis.
CC   -!- DISRUPTION PHENOTYPE: Cells produce only the non-phosphorylated
CC       variants CDA3b and CDA4b, while S.coelicolor strain A3(2) / 2377
CC       produces D-3-phosphohydroxyasparagine-containing peptide CDA2b as the
CC       major product, along with a minor amount of D-3-hydroxyasparagine
CC       variants CDA4b and CDA3b. {ECO:0000269|PubMed:17322197}.
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DR   EMBL; AL939115; CAB38878.1; -; Genomic_DNA.
DR   PIR; T36182; T36182.
DR   RefSeq; NP_627446.1; NC_003888.3.
DR   RefSeq; WP_011028845.1; NZ_VNID01000025.1.
DR   AlphaFoldDB; Q9Z4Z7; -.
DR   STRING; 100226.SCO3234; -.
DR   GeneID; 1098668; -.
DR   KEGG; sco:SCO3234; -.
DR   PATRIC; fig|100226.15.peg.3298; -.
DR   eggNOG; COG0510; Bacteria.
DR   HOGENOM; CLU_927217_0_0_11; -.
DR   UniPathway; UPA00979; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis; Kinase; Reference proteome; Transferase.
FT   CHAIN           1..300
FT                   /note="3-hydroxyasparagine phosphotransferase"
FT                   /id="PRO_0000350725"
SQ   SEQUENCE   300 AA;  33186 MW;  6FFD9572CF8A47F0 CRC64;
     MKTESDVQTG APTAADGALI ALAREVCPGF APGEVVYRSR TSLVVGGELD GVEALAKVRT
     PDWRRQCLRE IDTYDLFDAV PPPVPVPRRF ASDRERAVLV MERLTGEVLA PDRFPVTPVS
     REDLAGVLEA VERLRHWRPA AAGAWAVDYR GMLEGVHAQG VFDDGHWADL LRLLELSGAP
     REFGHGDLVL ANVVRSRGRQ VLIDWASSAL YLPGLDLAQL WMLLGDVPGA RARIEVEVAD
     RADDRDGMMP FLVNLTLLLY RERRAHRRFT DDASRARAVG LDAAWELTRH RVRQCLATAG