ID A0A3G8ZLQ8_9ACTN Unreviewed; 482 AA.
AC A0A3G8ZLQ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-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=EH165_09110 {ECO:0000313|EMBL:AZI58272.1};
OS Nakamurella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=1902245 {ECO:0000313|EMBL:AZI58272.1, ECO:0000313|Proteomes:UP000268084};
RN [1] {ECO:0000313|EMBL:AZI58272.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI58272.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Da X.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AZI58272.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI58272.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Peng F.;
RT "Nakamurella antarcticus sp. nov., isolated from Antarctica South Shetland
RT Islands soil.";
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; CP034170; AZI58272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8ZLQ8; -.
DR KEGG; nak:EH165_09110; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000268084; 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; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 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:UP000268084}.
FT DOMAIN 327..334
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 259
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT ACT_SITE 333
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ SEQUENCE 482 AA; 49080 MW; 51FC9870C40DDFA0 CRC64;
MSSAALSAAN PVTAAVEALV IGLYASDDGP IAADPALGDL AELLAVAGAT GRPGETTVIP
APAHYKALRI VGAGLGPQSD LTPERIRKAA GAASRALAGN RSVGSLLSRL NIGAAAEGHL
LGAYVFDAYK EPKKQPVEKF VLFTEANSAA NKSILRRAVI GAEAVGLARD LVNTAPNDLP
PAVFAQRANA AATEAGLKVE ILDEKALAKG GYGGILGVGA GSSRPPRLVR ITYTPTRSKA
TVALIGKGIT FDSGGLSIKP AAGMDHMTSD MSGAAAVVAT VIAAAALKLP ITITATAPLA
ENLPSGSSYR PGDVLTHFGG KTVHVLNTDA EGRLVLADAI VRAVQDKPDF LIETSTLTGA
QVVALGNRTM GVMGTEAFRD RIALLAREVG EGGWAMPMPE ELREGLDSAI ADIANVAGDR
AGGMLVAAHY LKEFVPEGLT WAHLDVAGPA FNTSKPYGYT GQGGTGIPVR TLLAVLEDIA
GA
//
