ID A0A1S2N450_9MICC Unreviewed; 506 AA. AC A0A1S2N450; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 14-DEC-2022, entry version 13. 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 ORFNames=BK826_00895 {ECO:0000313|EMBL:OIJ37007.1}; OS Rothia kristinae. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia. OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OIJ37007.1, ECO:0000313|Proteomes:UP000179540}; RN [1] {ECO:0000313|EMBL:OIJ37007.1, ECO:0000313|Proteomes:UP000179540} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LCT-H5 {ECO:0000313|EMBL:OIJ37007.1, RC ECO:0000313|Proteomes:UP000179540}; RA Huang B.; RT "Draft genome sequence of strain LCT isolated from the Shenzhou X RT spacecraft of China."; RL Submitted (OCT-2016) 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: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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OIJ37007.1}. 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; MODZ01000001; OIJ37007.1; -; Genomic_DNA. DR RefSeq; WP_075513929.1; NZ_MODZ01000001.1. DR AlphaFoldDB; A0A1S2N450; -. DR EnsemblBacteria; OIJ37007; OIJ37007; BK826_00895. DR Proteomes; UP000179540; Unassembled WGS sequence. 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; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR SUPFAM; SSF52949; Macro domain-like; 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 347..354 FT /note="CYTOSOL_AP" FT /evidence="ECO:0000259|PROSITE:PS00631" FT ACT_SITE 279 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT ACT_SITE 353 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 267 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 272 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 272 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 290 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 349 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 351 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" SQ SEQUENCE 506 AA; 52353 MW; 30D14ED92859C1A0 CRC64; MTESHDLALS VTAPDDGLEV RALVVGVLPA GQGARLAPHH LPEETAEGLQ AVLSDLGITG ARDEVHRLPG AESTGADVLV LVGLGELPEE GRERLDALRY AAGSAIRQLQ GMDTAALDLP VADLAEVGAL AEGAAFGAFV DPMYRTGTAD RELSPVGEVV ILTDVEAQEA EPVLTRALIL GEAVDSTRRL VNEAPNHLYP DSFAGRVLER VAGIDDVEVE VLDEQALAEG GFGGILGVGR GSHRPPRLVV VDYRPEGAGQ HMALVGKGIT FDSGGLSLKP GTGMMTMKSD MAGAAAVLNA VAAAAELRLP LRVTGYLCLA ENLPGGGATR PEDVLVMRGG TTVEVLNTDA EGRLVMADGL AYASEQSPDC LLDVATLTGA QVVALGERYA AVMGEDSLRE AVAQAGAEAG EPFWPMPLPE ELRAGLKSPV ADLKNIGAGR AGGMLTAGLF LQRFVGQVDG QPIPWAHLDI AGPSFNEGSE YGFTPKQGTG VAVRTLITLA ERIAAA //