ID A0A0J6ZKF5_9FIRM Unreviewed; 483 AA.
AC A0A0J6ZKF5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AB840_14215 {ECO:0000313|EMBL:KMO85316.1};
OS Megasphaera cerevisiae DSM 20462.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO85316.1, ECO:0000313|Proteomes:UP000036503};
RN [1] {ECO:0000313|EMBL:KMO85316.1, ECO:0000313|Proteomes:UP000036503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO85316.1,
RC ECO:0000313|Proteomes:UP000036503};
RA Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA Samadpour M.;
RT "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT type strain 20462.";
RL Submitted (JUN-2015) 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}.
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:KMO85316.1}.
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DR EMBL; LEKT01000074; KMO85316.1; -; Genomic_DNA.
DR RefSeq; WP_048515506.1; NZ_LEKT01000074.1.
DR AlphaFoldDB; A0A0J6ZKF5; -.
DR STRING; 39029.BSR42_05445; -.
DR PATRIC; fig|1122219.3.peg.3199; -.
DR InParanoid; A0A0J6ZKF5; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000036503; 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 PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 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:UP000036503}.
FT DOMAIN 330..337
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 262
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT ACT_SITE 336
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 332
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ SEQUENCE 483 AA; 52896 MW; C8275CE6D63C759C CRC64;
MITCNSSGSV DSMVVGVDQR MIILSRIPKE DAALIQAYTE KHINTLHYTS LQTFHCFVEG
RLKTYFLVGL DHKPIHYSTH EDFLMAKRIM AAAMKDGVSE LAVMVDTLDM DVASLIDGLL
YRNYEFTHYK TKAKSQTIRN INLITSSLKI KDFNTMCYVY TAIYEGIYVA RDLVNMPPND
LTPRKFADII TSMVKGDNIT IESLNKWALE KRKMGGIVAV GKGSMNPPQL LAIAYQGDPD
STAVLGVVGK GVTYDSGGIS LKSHANLEFM KTDMAGAAAA VGVIRALMLL KYPVNVLAVL
PLVENLPSSM SYHVDDIITM YDGKTVEIKN TDAEGRLILA DAVTYAQEKG ATRVIDLATL
TGACVTALGT VRSGMVGNDQ EWMNRLFNIS ERVHEKVWQF PADREYEEQL KSDVADLKNT
GGSEAGAVTA GLFIKQFVKS DTAWIHLDIA GTAFCEKKDE TGFVGATGVG IKSILELLKG
GIQ
//
