ID A0A127NUZ0_9CORY Unreviewed; 527 AA.
AC A0A127NUZ0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Metalloenzyme superfamily protein {ECO:0000313|EMBL:AMO89247.1};
GN ORFNames=WM42_1523 {ECO:0000313|EMBL:AMO89247.1};
OS Corynebacterium simulans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=146827 {ECO:0000313|EMBL:AMO89247.1, ECO:0000313|Proteomes:UP000074804};
RN [1] {ECO:0000313|EMBL:AMO89247.1, ECO:0000313|Proteomes:UP000074804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PES1 {ECO:0000313|EMBL:AMO89247.1,
RC ECO:0000313|Proteomes:UP000074804};
RX PubMed=26861018;
RG NISC Comparative Sequencing Program;
RA Tsai Y.C., Conlan S., Deming C., Segre J.A., Kong H.H., Korlach J., Oh J.;
RT "Resolving the Complexity of Human Skin Metagenomes Using Single-Molecule
RT Sequencing.";
RL MBio 7:e01948-15(2016).
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|RuleBase:RU003946}.
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DR EMBL; CP014634; AMO89247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127NUZ0; -.
DR STRING; 146827.WM42_1523; -.
DR KEGG; csp:WM42_1523; -.
DR PATRIC; fig|146827.5.peg.1500; -.
DR Proteomes; UP000074804; 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; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Magnesium {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|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..527
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007276517"
FT TRANSMEM 489..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 527 AA; 55751 MW; E24DDE01002942A8 CRC64;
MRNFSRALRV SVAAVATTAL TTGLVAPAHA AASGPKNIIY MIGDGMGYGH IASNNLYESG
QSKYLVEGAF GPDTAKELEG ESVQAFEDFN RLSMTTFPHG GSYDPAKAWS DHEYIKQGPT
DSAAAGTAMA TGSKVDNGTL GVSSYGHEME NLSERAIREG KSAGVVTSVP FDHATPAAFA
AHNKNRNNYL EIGDSMINSD LSVIMGAGHP KYNDDAQKVA AGSEDYSYIS KENLAALRDG
SKGWEFTDNT AGFESLAAGN AEEGKKYFGL APVATTLQQN RSGDAEAKEP GTDPKNDVVD
LPTMTNGALN ALGQDEDGFS LMIEGGAIDW SGHANQTGRD IEEVQDFNAA VDAAIDWVEK
NSSWEETLLI VTADHETGYL SGKDETDAWK PQTGTKGTAP THEWYSTNHT NQVVPFFFKG
AGSEDIQAKV SGTDPVRGEY IDNTTVAKLA LDEWWFNTAE DDTNNPGDTD NKPSNDGSSD
GSSSAGAGLA GAGVMALIFG IITAAAQALG LVKFDFKALQ DLIKQFA
//
