ID A0A1S2N450_9MICC Unreviewed; 506 AA. AC A0A1S2N450; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 08-MAY-2019, entry version 7. 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 CC turnover of intracellular proteins. Catalyzes the removal of CC unsubstituted N-terminal amino acids from various peptides. CC {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00727879}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which CC Xaa is preferably Leu, but may be other amino acids including CC Pro although not Arg or Lys, and Yaa may be Pro. Amino acid CC amides and methyl esters are also readily hydrolyzed, but rates CC on arylamides are exceedingly low.; EC=3.4.11.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181, CC ECO:0000256|SAAS:SAAS01118307}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, preferentially CC leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC 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 ECO:0000256|SAAS:SAAS00759153}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00754360}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000179540; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule. DR CDD; cd00433; Peptidase_M17; 1. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. 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 PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754331, ECO:0000313|EMBL:OIJ37007.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000179540}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00759165}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754382}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00727876}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754372}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00754389}. FT DOMAIN 347 354 CYTOSOL_AP. {ECO:0000259|PROSITE: FT PS00631}. FT ACT_SITE 279 279 {ECO:0000256|HAMAP-Rule:MF_00181}. FT ACT_SITE 353 353 {ECO:0000256|HAMAP-Rule:MF_00181}. FT METAL 267 267 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 272 272 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 272 272 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 290 290 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 349 349 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 351 351 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_00181}. FT METAL 351 351 Manganese 2. {ECO:0000256|HAMAP-Rule: FT 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 //