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Database: UniProt
Entry: A0A3Q9G3I2_9ACTO
LinkDB: A0A3Q9G3I2_9ACTO
Original site: A0A3Q9G3I2_9ACTO 
ID   A0A3Q9G3I2_9ACTO        Unreviewed;       495 AA.
AC   A0A3Q9G3I2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=EJ997_02260 {ECO:0000313|EMBL:AZQ78100.1};
OS   Flaviflexus ciconiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Flaviflexus.
OX   NCBI_TaxID=2496867 {ECO:0000313|EMBL:AZQ78100.1, ECO:0000313|Proteomes:UP000280344};
RN   [1] {ECO:0000313|EMBL:AZQ78100.1, ECO:0000313|Proteomes:UP000280344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H23T48 {ECO:0000313|EMBL:AZQ78100.1,
RC   ECO:0000313|Proteomes:UP000280344};
RA   Bae J.-W., Lee J.-Y.;
RT   "Complete genome sequence of Flaviflexus sp. H23T48.";
RL   Submitted (DEC-2018) 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; CP034593; AZQ78100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9G3I2; -.
DR   KEGG; flh:EJ997_02260; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000280344; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280344}.
FT   DOMAIN          341..348
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         266
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         266
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         284
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         343
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         345
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   495 AA;  51105 MW;  C9FC6D4F49EDDC21 CRC64;
     MIDVSELNFI QQAPDKTTAN VLVVPVVTGA DGVHAHVADL SKKAVTSLDA LLPTLGVSGK
     LGSLTRIPAP SGFSAETIAF VGTGKDADAL EATDLREAFG AAVRGLSHVS HVALAVASDD
     PEALYQAGLG GLLGAYTFGD YKVQPAPAEQ ITVVSPAKLK KAEFDALADE AEIVAEAVCE
     VRNLVNIPAS DLTPVKFADI AEAYGKSEKS LSVRVWDENE LEKDGFGGIL GVGQGSVNPP
     RLVRVEYKAR GAKSTLALVG KGITFDSGGL SIKPAKSMET MKTDMTGAAT VLETVVAASR
     LGVKTNLVAW LCLAENMPSG SATRPGDVLT MYSGRTVEVN NTDAEGRLVL GDGLARAVEE
     KPDAVIDVAT LTGAQIVALG GRISGVMGTD ETRNEIIEAA DAAGEDMWPM PLPDHLKSGF
     DSLVADTKNS GGRGGGMLSA GLFLAEFVGD TPWAHIDIAG PSFNEEGPFG STPKGGTGVA
     VQTLLAWIES HTAEA
//
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