AMPA_ECOLI
ID AMPA_ECOLI Reviewed; 503 AA.
AC P68767; P11648; Q2M649;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Aminopeptidase A/I;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; Synonyms=carP, xerB; OrderedLocusNames=b4260, JW4217;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=2670557; DOI=10.1002/j.1460-2075.1989.tb03547.x;
RA Stirling C.J., Colloms S., Collins J.F., Szatmari G., Sherratt D.J.;
RT "xerB, an Escherichia coli gene required for plasmid ColE1 site-specific
RT recombination, is identical to pepA, encoding aminopeptidase A, a protein
RT with substantial similarity to bovine lens leucine aminopeptidase.";
RL EMBO J. 8:1623-1627(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7616564; DOI=10.1006/jmbi.1995.0385;
RA Charlier D., Hassanzadeh G., Kholti A., Gigot D., Pierard A.,
RA Glansdorff N.;
RT "carP, involved in pyrimidine regulation of the Escherichia coli
RT carbamoylphosphate synthetase operon encodes a sequence-specific DNA-
RT binding protein identical to XerB and PepA, also required for resolution of
RT ColEI multimers.";
RL J. Mol. Biol. 250:392-406(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
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 [5]
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 [6]
RP MUTAGENESIS OF GLU-354.
RX PubMed=8057849; DOI=10.1111/j.1365-2958.1994.tb01013.x;
RA McCulloch R., Burke M.E., Sherratt D.J.;
RT "Peptidase activity of Escherichia coli aminopeptidase A is not required
RT for its role in Xer site-specific recombination.";
RL Mol. Microbiol. 12:241-251(1994).
RN [7]
RP FUNCTION IN PEPTIDE DEGRADATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=20067529; DOI=10.1111/j.1574-6968.2009.01879.x;
RA Hayashi M., Tabata K., Yagasaki M., Yonetani Y.;
RT "Effect of multidrug-efflux transporter genes on dipeptide resistance and
RT overproduction in Escherichia coli.";
RL FEMS Microbiol. Lett. 304:12-19(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10449417; DOI=10.1093/emboj/18.16.4513;
RA Strater N., Sherratt D.J., Colloms S.D.;
RT "X-ray structure of aminopeptidase A from Escherichia coli and a model for
RT the nucleoprotein complex in Xer site-specific recombination.";
RL EMBO J. 18:4513-4522(1999).
CC -!- FUNCTION: Probably involved in the processing and regular turnover of
CC intracellular proteins (PubMed:20067529). Catalyzes the removal of
CC unsubstituted N-terminal amino acids from various peptides. Required
CC for plasmid ColE1 site-specific recombination but not in its
CC aminopeptidase activity. Could act as a structural component of the
CC putative nucleoprotein complex in which the Xer recombination reaction
CC takes place (PubMed:8057849). {ECO:0000269|PubMed:8057849,
CC ECO:0000305|PubMed:20067529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC but not glutamic or aspartic acids.; EC=3.4.11.10;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by zinc and EDTA.
CC -!- SUBUNIT: Homohexamer.
CC -!- DISRUPTION PHENOTYPE: A quadruple peptidase disruption (pepA, pepB,
CC pepD and pepN) does not grow in M9 minimal medium, grows better when
CC supplemented with casamino acids (PubMed:20067529).
CC {ECO:0000269|PubMed:20067529}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- CAUTION: The ligation for manganese is based on the ligation for zinc,
CC an inhibitor, in the crystallographic structure reported in
CC PubMed:10449417. The ligation for manganese in the active form of the
CC enzyme may differ. {ECO:0000305}.
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DR EMBL; X15130; CAA33225.1; -; Genomic_DNA.
DR EMBL; X86443; CAA60164.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97157.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77217.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78257.1; -; Genomic_DNA.
DR PIR; S04462; APECA.
DR RefSeq; NP_418681.1; NC_000913.3.
DR RefSeq; WP_000397144.1; NZ_STEB01000013.1.
DR PDB; 1GYT; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-503.
DR PDBsum; 1GYT; -.
DR AlphaFoldDB; P68767; -.
DR SMR; P68767; -.
DR BioGRID; 4262726; 44.
DR DIP; DIP-47860N; -.
DR IntAct; P68767; 5.
DR STRING; 511145.b4260; -.
DR MEROPS; M17.003; -.
DR MoonProt; P68767; -.
DR jPOST; P68767; -.
DR PaxDb; P68767; -.
DR PRIDE; P68767; -.
DR EnsemblBacteria; AAC77217; AAC77217; b4260.
DR EnsemblBacteria; BAE78257; BAE78257; BAE78257.
DR GeneID; 66671821; -.
DR GeneID; 948791; -.
DR KEGG; ecj:JW4217; -.
DR KEGG; eco:b4260; -.
DR PATRIC; fig|1411691.4.peg.2444; -.
DR EchoBASE; EB0688; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_6; -.
DR InParanoid; P68767; -.
DR OMA; MKNTGPR; -.
DR PhylomeDB; P68767; -.
DR BioCyc; EcoCyc:EG10694-MON; -.
DR BioCyc; MetaCyc:EG10694-MON; -.
DR BRENDA; 3.4.11.1; 2026.
DR EvolutionaryTrace; P68767; -.
DR PRO; PR:P68767; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0001073; F:transcription antitermination factor activity, DNA binding; IMP:EcoliWiki.
DR GO; GO:0043171; P:peptide catabolic process; IMP:EcoliWiki.
DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoliWiki.
DR GO; GO:0042150; P:plasmid recombination; IMP:EcoliWiki.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Hydrolase;
KW Manganese; Metal-binding; Protease; Reference proteome.
FT CHAIN 1..503
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165750"
FT ACT_SITE 282
FT /evidence="ECO:0000255"
FT ACT_SITE 356
FT /evidence="ECO:0000255"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MUTAGEN 354
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8057849"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1GYT"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 167..192
FT /evidence="ECO:0007829|PDB:1GYT"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:1GYT"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 295..310
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 313..325
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:1GYT"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:1GYT"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:1GYT"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:1GYT"
FT HELIX 486..496
FT /evidence="ECO:0007829|PDB:1GYT"
SQ SEQUENCE 503 AA; 54880 MW; 643DED17EAC44DCD CRC64;
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI
AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG
QGSQNESLMS VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL
PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
ATGRPVALLA QFLLNRAGFN GEE
