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Database: UniProt/TrEMBL
Entry: Q639W1_BACCZ
LinkDB: Q639W1_BACCZ
Original site: Q639W1_BACCZ 
ID   Q639W1_BACCZ            Unreviewed;       557 AA.
AC   Q639W1;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:AAU17542.1};
DE            EC=3.1.3.1 {ECO:0000313|EMBL:AAU17542.1};
GN   Name=phoB {ECO:0000313|EMBL:AAU17542.1};
GN   OrderedLocusNames=BCE33L2719 {ECO:0000313|EMBL:AAU17542.1};
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU17542.1, ECO:0000313|Proteomes:UP000002612};
RN   [1] {ECO:0000313|Proteomes:UP000002612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA   Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA   Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU17542.1; -; Genomic_DNA.
DR   RefSeq; WP_000497804.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q639W1; -.
DR   KEGG; bcz:BCE33L2719; -.
DR   PATRIC; fig|288681.22.peg.2743; -.
DR   OMA; MMVMDGT; -.
DR   Proteomes; UP000002612; Chromosome.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 1.10.1200.140; Alkaline phosphatase, crown domain; 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   InterPro; IPR042085; Ap_crown.
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   Hydrolase {ECO:0000313|EMBL:AAU17542.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601952-2}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..557
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039404257"
FT   ACT_SITE        93
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ   SEQUENCE   557 AA;  60382 MW;  22C2902EF681C136 CRC64;
     MFVLGLKMKK LLLVGTMTLS MFCTVSMTNN HTVEAKVKKV ERQPKNVIIM VMDGTSSSAT
     TLARLYKGKP LALDEIVTGG VRTYSAESAI TDSAPAATAL ATGNKSNSGY VGVLPTIVSS
     PGLKPMKEED KLRPVANVLE GAKRTGRATG IVATAEIQHA TPAGFSAHHV NRNNFEVLAE
     QQVYQNIDVV LGGGKAALLP ETDSGIRKDG GDLVKVIKNK GYDFVETKEA LLGSKSNKIW
     GSFSLNALAF DMDREATNPE QPTLSQMTEK AIQTLSKDKD GFFLFVEGSK PDWAAHVNDP
     IGMISDVLAF DNAVAEALKF AKKDGNTMLI AVADHGNSGI SIGNMNTTKG YNTTPVSAYI
     YPLKKAKMTL EGTINNLKAD ISNVEEVAKL YGLDNLTYDE KERLKTAKKK IDVGPIFTTL
     LSKRANIGFT TGGHTGEDVF LYSYGPQKPY GLIQNTDVAK TMAKAMGFNL EKVTNKLFVE
     SESAFKQNGA TVTIDKTDVA NPVLIVKRNN VTAQLFVNKN IIRIKNKEYE LGSVVVESNG
     KVYVPEEAIH LFRKHSR
//
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