ID K4R2K7_STRDJ Unreviewed; 546 AA.
AC K4R2K7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Alkaline phosphatase D {ECO:0000313|EMBL:CCK30521.1};
DE EC=3.1.3.1 {ECO:0000313|EMBL:CCK30521.1};
GN Name=phoD3 {ECO:0000313|EMBL:CCK30521.1};
GN ORFNames=BN159_6142 {ECO:0000313|EMBL:CCK30521.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK30521.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK30521.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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DR EMBL; HE971709; CCK30521.1; -; Genomic_DNA.
DR RefSeq; WP_015660857.1; NC_020504.1.
DR AlphaFoldDB; K4R2K7; -.
DR STRING; 1214101.BN159_6142; -.
DR KEGG; sdv:BN159_6142; -.
DR PATRIC; fig|1214101.3.peg.6224; -.
DR eggNOG; COG3540; Bacteria.
DR HOGENOM; CLU_015982_2_1_11; -.
DR OrthoDB; 327733at2; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07389; MPP_PhoD; 1.
DR Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018946; PhoD-like_MPP.
DR InterPro; IPR038607; PhoD-like_sf.
DR InterPro; IPR032093; PhoD_N.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR Pfam; PF09423; PhoD; 1.
DR Pfam; PF16655; PhoD_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCK30521.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043}.
FT DOMAIN 65..161
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 174..515
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
SQ SEQUENCE 546 AA; 60737 MW; 9878341D0B459A3C CRC64;
MTLDTHPSRH TAELRAAARH LGRRRFLTVT GAAAALAFAV NLPTAGVAGA AELDAARITD
DPFTLGVASG DPQPGSVLLW TRLAPAPFQP DGGLPAERVT VHWELARDEN FRRTVRRGTA
TAHPEFQHTV HVEVGRLDTD RVFYYRFRVG SWISETGRTR TAPAPGDRVL GLKLAAVSCQ
AYHDGYFTPY AHLAADDVDV VLHLGDYLYE YAVSAAGGSR NYTDRTLPAL FNRETLTLED
YRLRYALYKS DPDLRAAHAA HPFVVTWDDH ETENNYADDI PENSVPPEEF LLRRASAYRA
YWEHQPLRRP QLPEGPDMQL YRRLHWGRLA QFDVLDTRQY RSNQAQGDGA KVPGPEVDDP
ARTMTGETQE RWLLDGWQDS RALWNVVPQQ VVFSQRKFDL TEPSRVSMDA WDGYRASRRR
ILDGAEAAGV ANLMVLTGDV HVGYAFDIKD DFDDPASRTR GTEIVATSIS SGRDGADKPA
NWDTYMTANP HLRFYNGRRG YVTVALGEEL ARADFKTVPY VTTPGAPVTT AASFVTEAGE
PGLKPA
//
