ID A0A8A5HZD8_ECOLX Unreviewed; 503 AA. AC A0A8A5HZD8; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE EC=3.4.11.1 {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE Short=LAP {ECO:0000256|HAMAP-Rule:MF_00181}; DE EC=3.4.11.10 {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181, GN ECO:0000313|EMBL:QTF35747.1}; GN ORFNames=JSU12_21810 {ECO:0000313|EMBL:QTF35747.1}; OS Escherichia coli O126:H45. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=2810407 {ECO:0000313|EMBL:QTF35747.1}; RN [1] {ECO:0000313|EMBL:QTF35747.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MIN10 {ECO:0000313|EMBL:QTF35747.1}; RA Majewski P.; RT "Plasmid mediated mcr-1.1 colistin-resistance in clinical extraintestinal RT Escherichia coli strains isolated in Poland."; RL Front. Microbiol. 0:0-0(2021). 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00000135, ECO:0000256|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:0000256|ARBA:ARBA00000967, ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00181}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP069677; QTF35747.1; -; Genomic_DNA. DR RefSeq; WP_000397144.1; NZ_CP069677.1. DR SMR; A0A8A5HZD8; -. DR GeneID; 66671821; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. 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 {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_00181}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00181}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00181}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00181}. FT DOMAIN 350..357 FT /note="CYTOSOL_AP" FT /evidence="ECO:0000259|PROSITE:PS00631" FT ACT_SITE 282 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT ACT_SITE 356 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 270 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 275 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 275 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 293 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 352 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 354 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT METAL 354 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" 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 //