ID A0A401IT73_9LACO Unreviewed; 841 AA.
AC A0A401IT73;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=pepN {ECO:0000313|EMBL:GBG94726.1};
GN ORFNames=LFYK43_11850 {ECO:0000313|EMBL:GBG94726.1};
OS Ligilactobacillus salitolerans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1808352 {ECO:0000313|EMBL:GBG94726.1, ECO:0000313|Proteomes:UP000286848};
RN [1] {ECO:0000313|Proteomes:UP000286848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK43 {ECO:0000313|Proteomes:UP000286848};
RA Tohno M., Tanizawa Y.;
RT "Draft genome sequences of Lactobacillus sp. YK43.";
RL Submitted (APR-2018) 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:GBG94726.1}.
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DR EMBL; BFFP01000016; GBG94726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401IT73; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000286848; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 9..178
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 214..432
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 507..818
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 373
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 841 AA; 94183 MW; E27B7D4E877BE82D CRC64;
MTRLYDDFKP TDYKVYLDID RSAKLITGQT EISGQALSAQ IAINQKFLKV ARVQVAGNDV
EFAVDDQAET IKVTLAQPGN TTLTIDYTAP LTDTMMGIYP SYYQVNGEKK QLIGTQFETT
AARQAFPCVD EPAAKATFEL AIKFDEHPGE TIIANMPETE VKDGVHYFEK TVKMSTYLVA
FAFGEMQSKL TQTKSGVQVG VFSTKAHQEN ELDFALDIAK RSIEFFEDFY HTPYPLPHSW
QLGLPDFSAG AMENWGLVTY REAYLVIDPE NTSLEVKERV ATVIAHELAH QWFGDLVTMQ
WWDDLWLNES FANMMEYVAI DALEPDWHIW ELFQTAEASA ALQRDATDGV QSVHVQVEEP
AEIDAIFDGA IVYAKGSRML VMVRALIGDD ALRQGLKAYF EAHQYGNATG ADLWDALGQA
AGIDLATIMN TWLEQPGYPV VSVQVVDGRL TLSQQQFFVG EGNEVGRLWQ IPLNGNYEAV
PQIMAEQTIE LGDYATLRAA AGQPLRLNLG NDSHFIVKYD DGLLEDILAN AKDLDAITQL
QLLQDLRLLA EGRQISYASV VPLLKDFADS KSNLVNVALY QITGNLKKFV QPDSTEESNL
RELFDQLSGA QVQRLGWQPK DGESIDDQLT RPYILNAALY AQNADAIAQG HALYLEKKYE
PASLPADTRP YILQNEVKNY GSPELFDQLL AEHGKTSDGN YQAGIEFALT KTSDQDLLAK
IVADFENSDV IRPQDLRGWY RDVLANDKGQ QAAWDWIRQE WQWLEKTVGG DMEFPTFITV
TAGVFHTPER LAEFKEFFTP KLDVSGLKRE IQMDTKVIES RVALIEDEKA AVNEAVAQAI
K
//
