ID A0A089LR24_9BACL Unreviewed; 573 AA.
AC A0A089LR24;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AIQ63981.1};
GN ORFNames=PSTEL_13675 {ECO:0000313|EMBL:AIQ63981.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ63981.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ63981.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ63981.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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 ---------------------------------------------------------------------------
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; CP009286; AIQ63981.1; -; Genomic_DNA.
DR RefSeq; WP_038695905.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LR24; -.
DR STRING; 169760.PSTEL_13675; -.
DR KEGG; pste:PSTEL_13675; -.
DR HOGENOM; CLU_008539_6_2_9; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000029507; Chromosome.
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; 1.10.60.40; -; 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 InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR Pfam; PF07833; Cu_amine_oxidN1; 1.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029507};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..573
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001846617"
FT DOMAIN 485..569
FT /note="Copper amine oxidase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07833"
FT ACT_SITE 104
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 573 AA; 60918 MW; 7F9B30F9994D0709 CRC64;
MKKSMKKAAI GGLACLILST GSFTYAAQSS SKSQAASKAP SKNLIVLIGD GMGPAQISAT
RYYEQYKKGV KHLNLDPYYV GQATTYADRG EDGGKVVSGV VTDSASAGTA FATGHKTYNA
GISVSNEDVS KPFASVIEAA ESSGKATGLV TTARITHATP AVYASHVRNR DNESAIASQY
IESGVDVLFG GGKQFFVTKD EKGKRTDKNI LPEFKAKGYT VVESASALKA LPASTTKVLG
LFGSSHVAYT PDRTAEIPSL AAMTSSALKI LSKDKNGFVM MIEGGRIDHA GHANDFPTLV
QETLDFDAAF KTAIEFAKKD GNTSVVVTAD HETGGLSLSR DNIYELNIDL WDKQKHSSES
IASKLAEAKS PEEIRSIVAE NTGFNDLTDE EVQAILAGDG SSYKQEGAYN AVISKRLLVG
WSGHGHSAVD VGVWAYGPIV EKVKGQVDNT QIARASAAIV GVNLDKRSAE LQSKYMYPKF
KINRDNEVLY PVAALIKSLG GSYSNGSTVS KASFGKNTLS IDMSKLTATL NGKAVSFTVD
NDNGTIYLPL SAFSQLTGKN LKWDSLSERI VLR
//
