ID A0A1E5P2M0_9ACTN Unreviewed; 540 AA.
AC A0A1E5P2M0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OEJ23737.1};
GN ORFNames=AS594_03835 {ECO:0000313|EMBL:OEJ23737.1};
OS Streptomyces agglomeratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ23737.1, ECO:0000313|Proteomes:UP000095759};
RN [1] {ECO:0000313|EMBL:OEJ23737.1, ECO:0000313|Proteomes:UP000095759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ23737.1,
RC ECO:0000313|Proteomes:UP000095759};
RA Chen X.;
RT "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL Submitted (AUG-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:OEJ23737.1}.
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DR EMBL; MEHJ01000001; OEJ23737.1; -; Genomic_DNA.
DR RefSeq; WP_069925659.1; NZ_MEHM01000001.1.
DR AlphaFoldDB; A0A1E5P2M0; -.
DR STRING; 285458.BGM19_32945; -.
DR OrthoDB; 327733at2; -.
DR Proteomes; UP000095759; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000095759};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039464759"
FT DOMAIN 59..155
FT /note="Phospholipase D N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16655"
FT DOMAIN 168..509
FT /note="PhoD-like phosphatase metallophosphatase"
FT /evidence="ECO:0000259|Pfam:PF09423"
FT REGION 340..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 59820 MW; 905619F4893C0FD0 CRC64;
MNSHQPELRA AVRRLGRRHF LTLTAAAAAL AFATELPAAG AASVPELDAR KITENPFTLG
LASGDPLPDS VVLWTRLAPR PLEPDSGLPE KRVVVTWELA HDEMFLRPVR GGTVTAHPEF
DHTLHVEVPG LDPDRPYYYR FRTGAWASPT GRTRTAPAAD TAKSQLKLAA VACQAYHHGY
YTPYRHLAGE DLDLVVHLGD YLYEYAVDSA GGARGYTDRL LPAHFDREAM TLADYRLRYA
LYKSDPDLAA AHAAHPFVVT WDDHETENNY AGGRSENNDP PEEFLLRRAG AYRAYWENQP
LRAPQRPRGP DMRLYRRLTF GRLAQFDILD TRQYRSERAY GGGWHKSGPE SEAASRTMTG
ETQERWLLDG WKGSGATWNV VPQQVTFARR RDVPTADFKL SMDAWDGYPA ARKRFLDGAE
AAGVQNLMVL DGDAHVGYGF DLKKDFDDPD SRTVATEIST TSVSSGKDGA DKPANFDSLV
QANPHLKFYN GRRGYTVITL GTDRARADFR TVSEVTRPGG TLTTAASFVT EAGRPGLIPA
//
