P21948 (PPB_ESCF3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkaline phosphatase
Short name=APase
EC=3.1.3.1

Gene names

Name:	phoA
Ordered Locus Names:	EFER_2640

Organism

Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]

Taxonomic identifier

585054 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia fergusonii

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	A phosphate monoester + H2O = an alcohol + phosphate.
Cofactor	Binds 1 magnesium ion. Binds 2 zinc ions.
Subunit structure	Homodimer.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the alkaline phosphatase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Magnesium Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alkaline phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21
	Chain	22 – 472	451	Alkaline phosphatase		PRO_0000024013
Sites
	Active site	125	1	Phosphoserine intermediate By similarity
	Metal binding	74	1	Magnesium By similarity
	Metal binding	74	1	Zinc 2 By similarity
	Metal binding	176	1	Magnesium By similarity
	Metal binding	178	1	Magnesium By similarity
	Metal binding	345	1	Magnesium By similarity
	Metal binding	350	1	Zinc 1 By similarity
	Metal binding	354	1	Zinc 1 By similarity
	Metal binding	392	1	Zinc 2 By similarity
	Metal binding	393	1	Zinc 2 By similarity
	Metal binding	435	1	Zinc 1 By similarity
Amino acid modifications
	Disulfide bond	191 ↔ 201		By similarity
	Disulfide bond	309 ↔ 359		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21948 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: EF956C964F931141	FASTA	472	49,430
	10 20 30 40 50 60 MKQSAIALAL LSCLITPVSQ AQTSQNINIL ENRAAQGDIT MPGGARRLSG DQTEALRASL 70 80 90 100 110 120 NDKPAKNIIL LIGDGMGDSE ITAARNYAEG AGGYFKGIDA LPLTGQYTHY ALDKKTGKPD 130 140 150 160 170 180 YVTDSAASAT AWTTGVKTYN GALGVDIHEN PHTTILEMAK AAGLATGNVS TAELQDATPA 190 200 210 220 230 240 ALVSHVTSRK CYGPSVTSEK CPGNALEKGG KGSITEQLLN ARADVTLGGG AKTFAETATA 250 260 270 280 290 300 GEWQGKTLRE QALARGYQIV SDAASLAAVT QAGQDKPLLG LFAEGNMPVR WHGPKASYHG 310 320 330 340 350 360 NLDKPAVTCT PNPQRNETVP TLAQMTDKAI ELLSKNERGF FLQVEGASID KQDHAANPCG 370 380 390 400 410 420 QIGETVDLDE AVQRALEFAK KDGNTLVIVT ADHAHSSQIV APDTKAPGLT QALNTKDGAV 430 440 450 460 470 MAISYGNSEE DSQEHTGSQL RIAAYGPNAA NVVGLTDQTD LFYTMKAALG LQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The molecular evolution of bacterial alkaline phosphatase: correlating variation among enteric bacteria to experimental manipulations of the protein." Dubose R.F., Hartl D.L. Mol. Biol. Evol. 7:547-577(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M33966 Genomic DNA. Translation: AAA24371.1. CU928158 Genomic DNA. Translation: CAQ90135.1.
PIR	I57445.
RefSeq	YP_002383746.1. NC_011740.1.
3D structure databases
ProteinModelPortal	P21948.
SMR	P21948. Positions 29-472.
ModBase	Search...
Protein-protein interaction databases
STRING	585054.EFER_2640.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ90135; CAQ90135; EFER_2640.
GeneID	7124018.
KEGG	efe:EFER_2640.
PATRIC	32129652. VBIEscFer122920_2555.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1785.
HOGENOM	HOG000099117.
KO	K01077.
ProtClustDB	PRK10518.
Enzyme and pathway databases
BioCyc	EFER585054:GJJM-2643-MONOMER.
Family and domain databases
Gene3D	3.40.720.10. 1 hit.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR001952. Alkaline_phosphatase. IPR018299. Alkaline_phosphatase_AS. IPR017850. Alkaline_phosphatase_core. [Graphical view]
Pfam	PF00245. Alk_phosphatase. 2 hits. [Graphical view]
PRINTS	PR00113. ALKPHPHTASE.
SMART	SM00098. alkPPc. 1 hit. [Graphical view]
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITE	PS00123. ALKALINE_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PPB_ESCF3

Accession

Primary (citable) accession number: P21948
Secondary accession number(s): B7LMK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program