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Database: UniProt
Entry: A0A3N1HNA8_9ACTN
LinkDB: A0A3N1HNA8_9ACTN
Original site: A0A3N1HNA8_9ACTN 
ID   A0A3N1HNA8_9ACTN        Unreviewed;       507 AA.
AC   A0A3N1HNA8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=EDC03_1537 {ECO:0000313|EMBL:ROP43940.1};
OS   Pseudokineococcus lusitanus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Pseudokineococcus.
OX   NCBI_TaxID=763993 {ECO:0000313|EMBL:ROP43940.1, ECO:0000313|Proteomes:UP000276232};
RN   [1] {ECO:0000313|EMBL:ROP43940.1, ECO:0000313|Proteomes:UP000276232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7306 {ECO:0000313|EMBL:ROP43940.1,
RC   ECO:0000313|Proteomes:UP000276232};
RX   PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
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:ROP43940.1}.
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DR   EMBL; RJKN01000003; ROP43940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1HNA8; -.
DR   InParanoid; A0A3N1HNA8; -.
DR   Proteomes; UP000276232; 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; 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:UP000276232}.
FT   DOMAIN          351..358
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         271
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         294
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         353
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         355
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         355
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   507 AA;  52211 MW;  F11A90E16328DF9F CRC64;
     MVDARMPRLV PVAGGDVRSA AGADVLAVPV ASAPPGEAEP QPRPGTADAA VWLGLNTAVL
     AEQQRFTGRA GETLGVPLPS ARDDGVGPRR LLLLGVGDGG ETALRRAGAA LARATRGADR
     VVTTAGTGLP PAALRAFAEG LLLAAYTPPR TGLEDGPRPA AEVVELLGVD DGPALPRAVA
     AARATWRTRD LASTPSSTKD PAWVAEQARA LAADLPGVEV EVLDADGLAR EGFGGLLAVG
     GGSASPPCLV TVRYRPPAGT PQRRHVVLVG KGITFDTGGL SLKPREAMVP MKTDMAGAAV
     VLATVLAAAE MRLPQPVTAL LPLAENALGG GSYRPGDVVR VHGGTTVEIA NTDAEGRMVL
     ADALSYADEQ LRPDLLVDVA TLTGAASLGL GRRHAALYTD DAPLLEQLRS ASAATGERVW
     RMPLVEDYTD ALESEVADLR HVAAAGGPSG GSITAALFLR EFVGRRRWAH LDIAGPGRAD
     KDEHEVTKGA TGFGTRLLLR WLEEGAV
//
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