ID B1MEC3_MYCA9 Unreviewed; 519 AA. AC B1MEC3; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 85. DE SubName: Full=Probable alkaline phosphatase {ECO:0000313|EMBL:CAM60187.1}; GN OrderedLocusNames=MAB_0087c {ECO:0000313|EMBL:CAM60187.1}; OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP OS 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium OS abscessus). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacteroides; Mycobacteroides abscessus. OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM60187.1, ECO:0000313|Proteomes:UP000007137}; RN [1] {ECO:0000313|EMBL:CAM60187.1, ECO:0000313|Proteomes:UP000007137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / RC TMC 1543 {ECO:0000313|Proteomes:UP000007137}; RX PubMed=19543527; DOI=10.1371/journal.pone.0005660; RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., RA Gaillard J.L.; RT "Non mycobacterial virulence genes in the genome of the emerging pathogen RT Mycobacterium abscessus."; RL PLoS ONE 4:E5660-E5660(2009). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2}; CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. CC {ECO:0000256|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU458896; CAM60187.1; -; Genomic_DNA. DR RefSeq; WP_005086146.1; NZ_MLCG01000005.1. DR AlphaFoldDB; B1MEC3; -. DR GeneID; 66970472; -. DR KEGG; mab:MAB_0087c; -. DR Proteomes; UP000007137; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro. DR CDD; cd16012; ALP; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR001952; Alkaline_phosphatase. DR InterPro; IPR018299; Alkaline_phosphatase_AS. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1. DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1. DR Pfam; PF00245; Alk_phosphatase; 2. DR PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601952-3}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..519 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002766550" FT TRANSMEM 493..514 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 25..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 131 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1" FT BINDING 77 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 182 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 184 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 353 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 362 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 400 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 401 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT BINDING 445 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2" FT DISULFID 197..207 FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3" FT DISULFID 313..367 FT /evidence="ECO:0000256|PIRSR:PIRSR601952-3" SQ SEQUENCE 519 AA; 53160 MW; 54D331945750C63F CRC64; MRIAHAATAV TSALTLALAP VAAAAPPSDA PEVPVGDIAK TGGANRTTGG RDGDKTADLR DSVRGRNAKN VILLIGDGMG TSEITSARNY QYGAAGTLPG LDALPITGEY TTFALTKDGP DKGKPDYVTD SAASGTGWAT GTKTYNGAIS VDLEGKPLDT ILEIVQRQGF ATGNVTTAEL QDATPAVLTA HVTDRDCKGP KETLARCAGN AVDNGGRGSI SEQLVNTRAD ISLGGGGKYF AETITAGEHK GKTSLEVAKA AGYQLPTTAG DLNKVNNLDN PVLGIFGTGN LPVQWDKVPA AVPNGGKLPP TVCRQNPDLP RDQPQLSAMT TKAIDLLVNS KKGKDKGFFL QVESASIDKQ DHAANICGQI GETIALDEAV AAAVDFARQD RNTLVIVTSD HGHSSLIVPD DFNSPTTLSV AVKTADGATM RIMYPTAPEG ESQTHTGTQV RIAAYGPGAA NVSGLTDQTD NFNTIVGALL GPKSPDAASG PSWWAAGGIA VVAAALGAAA AFLVGKRQT //