IAP_ECOLI
ID IAP_ECOLI Reviewed; 345 AA.
AC P10423; Q2MA76;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Alkaline phosphatase isozyme conversion protein;
DE EC=3.4.11.-;
DE Flags: Precursor;
GN Name=iap; OrderedLocusNames=b2753, JW2723;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3316184; DOI=10.1128/jb.169.12.5429-5433.1987;
RA Ishino Y., Shinagawa H., Makino K., Amemura M., Nakata A.;
RT "Nucleotide sequence of the iap gene, responsible for alkaline phosphatase
RT isozyme conversion in Escherichia coli, and identification of the gene
RT product.";
RL J. Bacteriol. 169:5429-5433(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
RC STRAIN=K12;
RX PubMed=1316900; DOI=10.1016/s0021-9258(19)50034-5;
RA Leyh T.S., Vogt T.F., Suo Y.;
RT "The DNA sequence of the sulfate activation locus from Escherichia coli K-
RT 12.";
RL J. Biol. Chem. 267:10405-10410(1992).
CC -!- FUNCTION: This protein, presumably an aminopeptidase, mediates the
CC conversion of E.coli alkaline phosphatase isozyme 1, to isozymes 2 and
CC 3 by removing, one by one, the two N-terminal arginine residues.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28C subfamily.
CC {ECO:0000305}.
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DR EMBL; M18270; AAA24005.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69263.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75795.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76830.1; -; Genomic_DNA.
DR EMBL; M74586; AAA23644.1; -; Genomic_DNA.
DR PIR; A28382; KZEC.
DR RefSeq; NP_417233.1; NC_000913.3.
DR RefSeq; WP_000490428.1; NZ_LN832404.1.
DR AlphaFoldDB; P10423; -.
DR SMR; P10423; -.
DR BioGRID; 4259465; 28.
DR STRING; 511145.b2753; -.
DR MEROPS; M28.005; -.
DR PaxDb; P10423; -.
DR PRIDE; P10423; -.
DR DNASU; 947215; -.
DR EnsemblBacteria; AAC75795; AAC75795; b2753.
DR EnsemblBacteria; BAE76830; BAE76830; BAE76830.
DR GeneID; 947215; -.
DR KEGG; ecj:JW2723; -.
DR KEGG; eco:b2753; -.
DR PATRIC; fig|1411691.4.peg.3987; -.
DR EchoBASE; EB0483; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_049425_1_0_6; -.
DR OMA; EATNWSL; -.
DR PhylomeDB; P10423; -.
DR BioCyc; EcoCyc:EG10488-MON; -.
DR BioCyc; MetaCyc:EG10488-MON; -.
DR PRO; PR:P10423; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0043687; P:post-translational protein modification; IMP:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000305"
FT CHAIN 25..345
FT /note="Alkaline phosphatase isozyme conversion protein"
FT /id="PRO_0000026855"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 37920 MW; 3DC433FB569E912D CRC64;
MFSALRHRTA ALALGVCFIL PVHASSPKPG DFANTQARHI ATFFPGRMTG TPAEMLSADY
IRQQFQQMGY RSDIRTFNSR YIYTARDNRK SWHNVTGSTV IAAHEGKAPQ QIIIMAHLDT
YAPLSDADAD ANLGGLTLQG MDDNAAGLGV MLELAERLKN TPTEYGIRFV ATSGEEEGKL
GAENLLKRMS DTEKKNTLLV INLDNLIVGD KLYFNSGVKT PEAVRKLTRD RALAIARSHG
IAATTNPGLN KNYPKGTGCC NDAEIFDKAG IAVLSVEATN WNLGNKDGYQ QRAKTPAFPA
GNSWHDVRLD NHQHIDKALP GRIERRCRDV MRIMLPLVKE LAKAS
