Entry ecoli: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-NOV-2009, entry version 49.
DE   RecName: Full=Cytosol aminopeptidase;
DE            EC=3.4.11.1;
DE   AltName: Full=Leucine aminopeptidase;
DE            Short=LAP;
DE   AltName: Full=Leucyl aminopeptidase;
DE   AltName: Full=Aminopeptidase A/I;
GN   Name=pepA; Synonyms=carP, xerB; OrderedLocusNames=b4260, JW4217;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=K12;
RX   MEDLINE=89356633; PubMed=2670557;
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-
RT   specific recombination, is identical to pepA, encoding aminopeptidase
RT   A, a protein with substantial similarity to bovine lens leucine
RT   aminopeptidase.";
RL   EMBO J. 8:1623-1627(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=95341674; 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
RT   resolution of 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   MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region 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   MEDLINE=97426617; 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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   MUTAGENESIS OF GLU-354.
RX   MEDLINE=94335644; PubMed=8057849;
RX   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
RT   required for its role in Xer site-specific recombination.";
RL   Mol. Microbiol. 12:241-251(1994).
RN   [7]
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
RT   for the nucleoprotein complex in Xer site-specific recombination.";
RL   EMBO J. 18:4513-4522(1999).
CC   -!- FUNCTION: Presumably involved in the processing and regular
CC       turnover of intracellular proteins. Catalyzes the removal of
CC       unsubstituted N-terminal amino acids from various peptides.
CC       Required for plasmid ColE1 site-specific recombination but not in
CC       its aminopeptidase activity. Could act as a structural component
CC       of the putative nucleoprotein complex in which the Xer
CC       recombination reaction takes place.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC       Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC       including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC       acid amides and methyl esters are also readily hydrolyzed, but
CC       rates on arylamides are exceedingly low.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by zinc and EDTA.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC   -!- CAUTION: The ligation for manganese is based on the ligation for
CC       zinc, an inhibitor, in the crystallographic structure reported in
CC       PubMed:10449417. The ligation for manganese in the active form of
CC       the enzyme may differ.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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; AP_004756.1; -.
DR   RefSeq; NP_418681.1; -.
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   STRING; P68767; -.
DR   MEROPS; M17.003; -.
DR   PRIDE; P68767; -.
DR   GeneID; 948791; -.
DR   GenomeReviews; AP009048_GR; JW4217.
DR   GenomeReviews; U00096_GR; b4260.
DR   KEGG; ecj:JW4217; -.
DR   KEGG; eco:b4260; -.
DR   EchoBASE; EB0688; -.
DR   EcoGene; EG10694; pepA.
DR   HOGENOM; P68767; -.
DR   OMA; LGHHNSG; -.
DR   BioCyc; EcoCyc:EG10694-MON; -.
DR   Genevestigator; P68767; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_00181; -; 1.
DR   InterPro; IPR011356; Peptidase_M17.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   InterPro; IPR008283; Peptidase_M17_N.
DR   PANTHER; PTHR11963:SF3; Peptidase_M17; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF02789; Peptidase_M17_N; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminopeptidase; Complete proteome;
KW   Direct protein sequencing; Hydrolase; Manganese; Metal-binding;
KW   Protease.
FT   CHAIN         1    503       Cytosol aminopeptidase.
FT                                /FTId=PRO_0000165750.
FT   ACT_SITE    282    282       Potential.
FT   ACT_SITE    356    356       Potential.
FT   METAL       270    270       Manganese 2 (Probable).
FT   METAL       275    275       Manganese 1 (Probable).
FT   METAL       275    275       Manganese 2 (Probable).
FT   METAL       293    293       Manganese 2 (Probable).
FT   METAL       352    352       Manganese 1 (Probable).
FT   METAL       354    354       Manganese 1 (Probable).
FT   METAL       354    354       Manganese 2 (Probable).
FT   MUTAGEN     354    354       E->A: Loss of activity.
FT   STRAND        2      6
FT   HELIX        10     12
FT   STRAND       18     23
FT   TURN         24     26
FT   HELIX        30     36
FT   STRAND       39     41
FT   HELIX        42     49
FT   STRAND       59     64
FT   STRAND       69     77
FT   HELIX        86    102
FT   STRAND      106    110
FT   HELIX       112    114
FT   HELIX       122    137
FT   STRAND      156    160
FT   HELIX       164    166
FT   HELIX       167    192
FT   TURN        195    197
FT   HELIX       200    213
FT   TURN        214    217
FT   STRAND      218    223
FT   HELIX       225    230
FT   HELIX       234    241
FT   STRAND      243    245
FT   STRAND      248    255
FT   STRAND      265    275
FT   HELIX       287    294
FT   HELIX       295    310
FT   STRAND      313    325
FT   STRAND      337    339
FT   STRAND      345    347
FT   HELIX       355    365
FT   HELIX       366    369
FT   STRAND      372    378
FT   HELIX       382    388
FT   TURN        389    391
FT   STRAND      392    398
FT   HELIX       400    413
FT   STRAND      417    419
FT   HELIX       424    427
FT   HELIX       428    430
FT   STRAND      433    439
FT   HELIX       446    455
FT   STRAND      463    467
FT   TURN        469    471
FT   STRAND      472    474
FT   HELIX       476    478
FT   HELIX       486    496
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         3    498       ihamap:Cytosol_peptidase_M17 [T]
FT   MYHIT       350    357       ipat:CYTOSOL_AP [T]
FT   MYHIT        19    147       ipfam:Peptidase_M17_N [T]
FT   MYHIT       186    489       ipfam:Peptidase_M17 [T]
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
//