ID Q5HKX9_STAEQ Unreviewed; 489 AA.
AC Q5HKX9;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Alkaline phosphatase family protein {ECO:0000313|EMBL:AAW53041.1};
GN OrderedLocusNames=SERP2208 {ECO:0000313|EMBL:AAW53041.1};
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW53041.1, ECO:0000313|Proteomes:UP000000531};
RN [1] {ECO:0000313|EMBL:AAW53041.1, ECO:0000313|Proteomes:UP000000531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531};
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J., Khouri H., Utterback T., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K., Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53041.1; -; Genomic_DNA.
DR RefSeq; WP_002437984.1; NC_002976.3.
DR AlphaFoldDB; Q5HKX9; -.
DR STRING; 176279.SERP2208; -.
DR KEGG; ser:SERP2208; -.
DR eggNOG; COG1785; Bacteria.
DR HOGENOM; CLU_008539_6_2_9; -.
DR Proteomes; UP000000531; 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 Reference proteome {ECO:0000313|Proteomes:UP000000531};
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..489
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004256684"
FT ACT_SITE 114
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 297
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 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 489 AA; 53361 MW; 39C4450EDA099C9E CRC64;
MKFMNKMGKT TLASSIVAAS VLSTVNVSYA SGSSEQSAQT KQTQNDAIAF GNTKNPKNVI
FMVGDGMGPS FNTAYRYYKN KPGAKKMTPT AFDKYLKGTN RTYSNDPKEN VTDSAAGGTA
FSTGHKTYNG AISVDTNKKP IKSVLEQAKE QGKSTGLVTT AELTDATPAV YAAHIDSRDK
KDEIAQQFYN DKINGKHKVD VMLGGGAKYF GKENKNLAKK FKKDGYDIVS NKDELNQSQS
KQVLGTFSEK DMPLQIDAPQ SNPLLVDMQN SALNKLSKNN KGFFLMVEGA SIDKAAHPND
ITGVMSEMSG FETAFDNAIN YAKTHKDTLV VATADHSTGG LSTAKGKDYK WNPEAIHKMK
HSGMYMTKQI ADGKDPEKVI KDGYGIDFPN KQLDKVKKAA DELHKLQKEG KDDKDEKVVE
QTTKLQNAIQ KPINDASHTG WTTNGHTGVD VNTYAYGPGS NKFKGNMENT QSAKNLFDFF
GDNVTSNQN
//
