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Database: UniProt
Entry: A0A1H2JE72_9ACTN
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ID   A0A1H2JE72_9ACTN        Unreviewed;       524 AA.
AC   A0A1H2JE72;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN04488563_2572 {ECO:0000313|EMBL:SDU54421.1};
OS   Jiangella alkaliphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC   Jiangella.
OX   NCBI_TaxID=419479 {ECO:0000313|EMBL:SDU54421.1, ECO:0000313|Proteomes:UP000182977};
RN   [1] {ECO:0000313|Proteomes:UP000182977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45079 {ECO:0000313|Proteomes:UP000182977};
RA   Varghese N.;
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}.
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DR   EMBL; LT629791; SDU54421.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2JE72; -.
DR   STRING; 419479.SAMN04488563_2572; -.
DR   Proteomes; UP000182977; Chromosome i.
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; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 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:SF23; CYTOSOL AMINOPEPTIDASE; 1.
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   SUPFAM; SSF53187; Zn-dependent exopeptidases; 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|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          367..374
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         287
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         292
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         292
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         310
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         369
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         371
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         371
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   524 AA;  53574 MW;  A892B1AA6ED3C046 CRC64;
     MSAESTVRPT EVMVDARPLL DAEAGVLALA VWPDDAPGPD GGDGDGSPWI GPGGAEVADA
     LGLDLFAALE RDRGSGKAGE VVSVPVYAEG RGAGSVDGEV DVVRVLLVGL GDGSAAAYRK
     AGAALARAAR GTDRLASAVT ATADDATTRA FVEGAVLATY ALGGFRDKPA PAAKRPLGTL
     VLAGDGARAD VVAAAVAVAG GSWTARDLAQ TPSNVKDPEW LAEQARRIGA EHRLDVRVRD
     EKALADEGFG GILAVGQGSE RPPRLIALRY EPPKAGRGTP HVVLVGKGIT YDSGGLSLKP
     REGMVPMKTD MTGGAVVMGV LSAVRELGVA VRVTGLVAAA ENMPGAGAQR PSDVIRQYDG
     TTVEVRNTDA EGRLVLADGI GYAVAELEPT VIVDVATLTG AATTALGRGL GALYSPSDEL
     AAALRSAGEA AGERLWRLPL VEDYRFGLES SIADVSHIDT EHLGGGSIIA ALFLQRFVGD
     LPWAHLDIAG PARAESDKLE LTKGGTGFGV RALLYWLEAG APVA
//
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