ID A0A1F1V189_9CORY Unreviewed; 1072 AA.
AC A0A1F1V189;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OFT32126.1};
GN ORFNames=HMPREF3171_00660 {ECO:0000313|EMBL:OFT32126.1};
OS Corynebacterium sp. HMSC08F01.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581139 {ECO:0000313|EMBL:OFT32126.1, ECO:0000313|Proteomes:UP000176366};
RN [1] {ECO:0000313|EMBL:OFT32126.1, ECO:0000313|Proteomes:UP000176366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08F01 {ECO:0000313|EMBL:OFT32126.1,
RC ECO:0000313|Proteomes:UP000176366};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OFT32126.1}.
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DR EMBL; LWNT01000012; OFT32126.1; -; Genomic_DNA.
DR RefSeq; WP_070482178.1; NZ_KV789270.1.
DR AlphaFoldDB; A0A1F1V189; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000176366; Unassembled WGS sequence.
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; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
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; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 2.
PE 3: Inferred from homology;
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1072
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039023566"
FT TRANSMEM 1037..1062
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 321..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 81
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 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 1072 AA; 111907 MW; 40A79E28B1B2B4F4 CRC64;
MRFSLKAATA VVSASALAIA NLPTSLAQSA EQSFNGKDTC ISIDSNGNIV APQPGDCTQF
GKGGQGNTDA QARNVIFILG DGMGHQEITA ARNYLKGANG RFEGLDELTA AGAYTTFAVG
KDGKRQYVTD SAASATGWST GTKTYNGALS VDITGKPHEN LLEMAKNAGM RTGNVSTAEI
QDATPGAMHS HISKRGYYAP SGDAKPVKGA EARENGGLGS ISEQIIDTRA DVTLGGGRKY
FDAEVQQGGE NRNPFLTDKN DGGVDWEAGK SVRENAIAKG YQVVDDKQGL EGITVANQDQ
PVLGLFHDKN MTRKFEQTVP VKSDGTTEPE VCKEADRGDE PSAAEMTKKA IELLDDKSAD
KGFFLQVESA SIDKADHAAD ACGMIGETQQ IDEVIKEALD FAKADGETMI VVTADHAHTA
EIIPDGRPSV SAVTRLKTPK DGTTMSIGFG TQPWLDENGN PVFDKKANGE PFDTPNFSMM
HTGTQVRIAG FGPGSENVNG QLDQTDAFYV MANALGLNGG TEGGQEPWKI NKGAKVASLA
NRSKAKPGDE LCYLVSAGEA PKVGDCAQFG TEGQGIDNSK AKNVVLLIGD GTGDSEITAA
RNYLKGSAGR FEGLDDLDYT GYLTTFSLDK ETGLPNYVGD SAATGTAWNS GVKTYNGAVG
VDNAGKPVAT LGEIAKAKGL KIGNVTTAEI QDATPAAFAA HAIKRSYYAP SGDKKVAEGE
QLRENGGLGS ISEQIVDLRA DVTLGGGRSY FNTEVVQGGQ WGENGNTWTA GKTVLENAKD
NGYQVVTNAS ELDAIAEANA DKPVLGLFSE GNMPRALNQS IPTTDGGDLE PATCVANPEF
TAETPRLAAM TSKALELLQN DKGFVLQVES ASPDKADHQA DACGLIGEVG QLDEAVQAVQ
DWVEKTGEET LIVATADHAH TAQITYENQN TAGRVTQLTT VEGSTMAVNF ATSKTNEDED
ALGGQQHTGA QLRVAASGPG AANLTGQIDQ TDLFFASLNA LGIDPVNHNL TFENKMQPVE
ETTEGDSAAG SSVDSPALIA TLAIAGIAGL ISLIALLAPF AVDGALGPIA KF
//
