AMPA_SHIB3
ID AMPA_SHIB3 Reviewed; 503 AA.
AC B2TYY4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181};
DE EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
GN Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181};
GN OrderedLocusNames=SbBS512_E4821;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC intracellular proteins. Catalyzes the removal of unsubstituted N-
CC terminal amino acids from various peptides. {ECO:0000255|HAMAP-
CC Rule:MF_00181}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00181};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00181};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC Rule:MF_00181}.
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DR EMBL; CP001063; ACD06458.1; -; Genomic_DNA.
DR RefSeq; WP_000397138.1; NC_010658.1.
DR AlphaFoldDB; B2TYY4; -.
DR SMR; B2TYY4; -.
DR STRING; 344609.SbBS512_E4821; -.
DR MEROPS; M17.003; -.
DR EnsemblBacteria; ACD06458; ACD06458; SbBS512_E4821.
DR KEGG; sbc:SbBS512_E4821; -.
DR HOGENOM; CLU_013734_2_2_6; -.
DR OMA; MKNTGPR; -.
DR Proteomes; UP000001030; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease.
FT CHAIN 1..503
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_1000098351"
FT ACT_SITE 282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT ACT_SITE 356
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 354
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ SEQUENCE 503 AA; 54879 MW; D72A5EFD636A5DF0 CRC64;
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAILHGLAI
AAAIKAAKDL 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
