ID A0A0R1GQU9_9LACO Unreviewed; 857 AA.
AC A0A0R1GQU9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=FD07_GL000871 {ECO:0000313|EMBL:KRK36399.1};
OS Levilactobacillus parabrevis ATCC 53295.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1267003 {ECO:0000313|EMBL:KRK36399.1, ECO:0000313|Proteomes:UP000051176};
RN [1] {ECO:0000313|EMBL:KRK36399.1, ECO:0000313|Proteomes:UP000051176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53295 {ECO:0000313|EMBL:KRK36399.1,
RC ECO:0000313|Proteomes:UP000051176};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK36399.1}.
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DR EMBL; AZCZ01000022; KRK36399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1GQU9; -.
DR STRING; 357278.IV61_GL000941; -.
DR PATRIC; fig|1267003.4.peg.924; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000051176; 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; 2.60.40.1910; -; 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 25..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 523..834
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 389
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 857 AA; 95198 MW; 3D47AEC464858505 CRC64;
MYNEDILIIQ EEIMAKSTHF YELFQPTHYN VYLDINRAAK SISGTSTITG DAKATSIAIH
QKFMTISAVK ADGQDVPFTF DDKSEGIHID LTKTGETTLA IDFTAPLTDS MMGIYPSYYD
VNGEKKLIIG TQFETTAARQ AFPCVDEPEA KATFDLAIKF DEHDGETIIS NMPETKTENG
VHYFDTTVRM STYLIAFAFG EMQSKLTTTK SGVQVGVFAT KAHQAKELDF ALDIAKRSIE
FYEDFYQTPY PLPHSWQMAL PDFSAGAMEN WGLVTYREAY LLLDPDNTSF ETKQRVATVI
AHELAHQWFG DLVTMKWWDD LWLNESFANM MEYVAINAIE PDWHIWEVFQ TTEAPMALQR
DATDGVQSVH VQVEDPAEID ALFDSAIVYA KGARMLVMVR ALIGDNALRQ GLKAYFAAHH
YGNATGADLW AALGDASGMN VGAIMNSWLE QPGYPVVSAA VVDGKLTITQ QQFFVGEGKD
AGRQWQVPLN SNYSAAPAIF ADQSATLGDY ATLRKASGEP FRLNVGNNSH FIVKYDDTLL
QDILANLDSL DAITQLQLLQ DLRLLAEGRQ ISYAAIVPLL DRFAASHSTV VNDVLYGVAS
NLKKFVTPDS TEEQQLQALF DKLSAKQVAR LGWTPKAGES NDDQLTRPYV LNATLYAKNA
ESIAAAHAVF VAHQDNPGTL PAATRVFILA NEIKHFGSDQ LFDQLLNDYR TSSDAGYKAD
LSSALPTTPD AKQIAKLITL FEDAETIKPQ DLRAWYRGVL GNDKGQQAAW DWIRNDWQWL
EDTVGGDMEF TTYITVTAGI FHTPARLAEF KAFFTPKINT PGLTREIKMD TKVIESRVDL
VEAEKDAVHA AVAKTVK
//
