ID A0A0H3JXN5_STAAM Unreviewed; 474 AA.
AC A0A0H3JXN5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Alkaline phosphatase III {ECO:0000313|EMBL:BAB58789.1};
GN Name=phoB {ECO:0000313|EMBL:BAB58789.1};
GN OrderedLocusNames=SAV2627 {ECO:0000313|EMBL:BAB58789.1};
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878 {ECO:0000313|EMBL:BAB58789.1, ECO:0000313|Proteomes:UP000002481};
RN [1] {ECO:0000313|EMBL:BAB58789.1, ECO:0000313|Proteomes:UP000002481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699 {ECO:0000313|Proteomes:UP000002481};
RX PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J., Ito T., Kanamori M., Matsumaru H.,
RA Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., Takahashi N.K.,
RA Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S.,
RA Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K.,
RA Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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}.
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DR EMBL; BA000017; BAB58789.1; -; Genomic_DNA.
DR RefSeq; WP_000953755.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JXN5; -.
DR SMR; A0A0H3JXN5; -.
DR KEGG; sav:SAV2627; -.
DR HOGENOM; CLU_008539_6_2_9; -.
DR PhylomeDB; A0A0H3JXN5; -.
DR Proteomes; UP000002481; 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 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.
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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..474
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002613165"
FT REGION 405..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 474 AA; 51921 MW; E6737A6D23310C64 CRC64;
MLSVKKATKF AVANLIIVST VFSSVTPAIA QSDKSSKDES FAVGNTKNPK NVIFLVGDGM
GPSFNTAYRY YKNDSHAKEM TPTAFDSYLK GTNRTYSNDP KQNITDSAAG GTAFSSGHKT
YNGAIGVDSN KQKVKTVLER AKEKGKSTGL VSTAELTDAT PAAYAAHVTS RDDKNEIAKQ
FYKDKINGKH KVDVLLGGGA KYFGKSNGNL DKKFKKDGYD LATNSKDLSK SDKDKVLGLF
ADKNMPLAID ASKDEPSLAD MQQSALSKLE RNKKGFFLMV EGASIDKSAH SNDITGVMSE
MEGFEKAFDD AIQYAKKHKD TLVVATADHS TGGLTIGKDK GYEWNPQPIK SMKHSGSYMT
EKMAKGEDPE KVINEGYGFE FSQDDMKKVK KENKKLQKLL KKEKDEKSAD VEKQTKALQH
AIQKPVNDKS YTGWTSDGHT GEDVNTYAYG PRSESFSGNI ENTESAKIIF DIFK
//
