ID I7JX52_9LACO Unreviewed; 841 AA.
AC I7JX52;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=BN53_09135 {ECO:0000313|EMBL:CCI84365.1};
OS Lactobacillus pasteurii DSM 23907 = CRBIP 24.76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI84365.1, ECO:0000313|Proteomes:UP000009311};
RN [1] {ECO:0000313|EMBL:CCI84365.1, ECO:0000313|Proteomes:UP000009311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311};
RA Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., Clermont D.;
RT "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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:CCI84365.1}.
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DR EMBL; CAKD01000001; CCI84365.1; -; Genomic_DNA.
DR RefSeq; WP_009558914.1; NZ_CAKD01000001.1.
DR AlphaFoldDB; I7JX52; -.
DR STRING; 1423790.BN53_09135; -.
DR MEROPS; M01.002; -.
DR PATRIC; fig|1423790.3.peg.1337; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000009311; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000009311};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 11..180
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 216..434
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 508..816
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 375
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 841 AA; 95046 MW; EA7073AC9B66D14C CRC64;
MAVKRIYETF HPEHYDLFID VNRKEKLITG TSTITGEAME TTIFVNEKYM TIKAVKADGQ
DVPFEVIDAD EVIKIDLPKT GKTTVAIDYS APLTDTMMGI YPSYYELNGE KKQIIGTQFE
TTFARQAFPS IDEPEAKATF TLALKWDEEE GEIALANMPE IKVEDGVHYF EETVRMSSYL
VAFAFGDLQS KMTETKSGVK IGVFATKAHQ AKELDFALDI AKRSIEFYED FYQTPYPLPH
SWQLALPDFS AGAMENWGLV TYREAYLTLD PDNTSLQMKK LVATVIAHEL AHQWFGDLVT
MKWWDNLWLN ESFANMMEYV AIDAIEPDWH IWEMFQSSEA AQALTRDATD GVQSVYVEVN
DPAEIDALFD GAIVYAKGSR MLVMVRALLG DEALRKGLKY YFDHHKFGNT TGDDLWDALS
TATDLNIGEI MHTWLNQPGY PVVNAFVEDG HLKLTQKQFF VGEGEEVGRK WAIPLNANFD
APQIMSETEL DLGNYEDLRK QAGEALRLNV GNSSHFIVKY DDTLMKDILA DVASLDPIAK
LQLLQDLRLL AEGRQISYAE IVPLLTKLAD DKSGLVNDAL YTTAAKLRQF VEVGSDEEKN
LKKLYDKLSA GQVARLGWEV KDSDSDDDQQ VRQDVLSASL YAENAASIKE AHELFEAHKD
DLYSLNADVR AHVIMNEVKN FPAAGLIDQL IDEYKKTSDA SYKLDLRVAI TKTKDEAEIA
KIIGYFKDAD VVKPQDLRGW FAGMLANDAS EEAAWTWIRD EWSWLDEKIG GDMEFATFIT
VVARQFRTAK RLAEFKEFFE PKLSQAMLTR EIKMDIKFIA ARVDLIESEK AAVNKAVEAS
L
//
