ID   A0A138AKB7_9ACTN        Unreviewed;       536 AA.
AC   A0A138AKB7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:KXP10812.1};
GN   ORFNames=AXK60_05900 {ECO:0000313|EMBL:KXP10812.1};
OS   Tsukamurella pseudospumae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=239498 {ECO:0000313|EMBL:KXP10812.1, ECO:0000313|Proteomes:UP000070258};
RN   [1] {ECO:0000313|Proteomes:UP000070258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15929 {ECO:0000313|Proteomes:UP000070258};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXP10812.1}.
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DR   EMBL; LSRF01000023; KXP10812.1; -; Genomic_DNA.
DR   RefSeq; WP_068571040.1; NZ_LSRF01000023.1.
DR   AlphaFoldDB; A0A138AKB7; -.
DR   STRING; 239498.AXK60_05900; -.
DR   OrthoDB; 3497025at2; -.
DR   Proteomes; UP000070258; Unassembled WGS sequence.
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:SF6; ALKALINE PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G03860); 1.
DR   PANTHER; PTHR43606; 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;
FT   DOMAIN          60..149
FT                   /note="Phospholipase D N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16655"
FT   DOMAIN          165..519
FT                   /note="PhoD-like phosphatase metallophosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF09423"
FT   REGION          38..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  57523 MW;  370E8682B76D9966 CRC64;
     MPLSDSPFSR RTALRAGAAG ALLVPAGALL SACGTSSDGA AASSSAGSTG LVRGRPSLTH
     GIASGDPRTD GALVWARSDA PARMIVETAS SESFSDPRRF EGPKLDPTSD GAGRFRITGL
     EPGQTVHYRV TLEGENGARS EPVAGTFRTA PSAAGNVKFL WSGDVVGQGW GINRDGGMAI
     MGAMADARPD FFIHSGDAIY ADNPVPETQK QNDGNIYRNV TAAAKNQVAQ TLDDFRGNFA
     YNLLDEHYRR FAATVPQLIQ WDDHEVVNNW YPGESLAGQN RKGYTETDVN KLAGSSYQAW
     REWQPVQPTE AADGRLYRKI SYGPLLDVFV LDMRSYKDPN PNNWATTDDG GILGAKQTQW
     LIDGLNGSTA TWKVVANDLP LSIVVPDSLS DPKDGPKSME AVAQGDNGAP LGREIAFSRI
     LSRTKDVKNV VYLTADVHYT AAISYHPDRA AYQDFSPFWE FVSGPLNAGA FPKSPLDGTF
     GAQYEFVHAP DKPNVSPAEG FQHFGEVTID SGSRALTVNL RDAKGASLYT KELTPA
//