ID A0A0R1PC81_9LACO Unreviewed; 844 AA.
AC A0A0R1PC81;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=FD27_GL000912 {ECO:0000313|EMBL:KRL27162.1};
OS Limosilactobacillus frumenti DSM 13145.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423746 {ECO:0000313|EMBL:KRL27162.1, ECO:0000313|Proteomes:UP000051445};
RN [1] {ECO:0000313|EMBL:KRL27162.1, ECO:0000313|Proteomes:UP000051445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13145 {ECO:0000313|EMBL:KRL27162.1,
RC ECO:0000313|Proteomes:UP000051445};
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:KRL27162.1}.
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DR EMBL; AZER01000016; KRL27162.1; -; Genomic_DNA.
DR RefSeq; WP_057750836.1; NZ_AZER01000016.1.
DR AlphaFoldDB; A0A0R1PC81; -.
DR STRING; 1423746.FD27_GL000912; -.
DR PATRIC; fig|1423746.3.peg.923; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000051445; 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 Reference proteome {ECO:0000313|Proteomes:UP000051445};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 12..181
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 217..435
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 510..821
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 376
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 844 AA; 95174 MW; 361AC226FE48C580 CRC64;
MSSIARFYEN FKPSHYDVFL DINRAKKTIK GNTTVSGIAE QPVIKLHQKD LTIESVQVAG
ENVPFKVDND AEAIIITLPE DGDVTLTVTY SAPLTDTMMG IYPSYYKVNG ETKQIIGTQF
ETTFARQAFP CVDEPEAKAT FSLAIKYDEH PGETIIANMP EDHESAGVHY FQQTVRMSTY
LVAFAFGELQ AKKTTTKSGV QVGVFATKAH QPKELDFALE IAKKAIEFYE DFYQTPYPLP
HSWQLALPDF SAGAMENWGL VTYREAYLLL DPDNTSLDMK RLVATVITHE LAHQWFGDLV
TMKWWDDLWL NESFANMMEY VAVDAIHPEW KIWELFQTSE APMALQRDAT DGVQPVHVQV
NNPAEIDAIF DAAIVYAKGA RMLVMVRSLI GDDALRAGLK NYFAAHKYHN ATGADLWSAL
GKASHLDIGD IMNSWLEQPG YPVVSASVED GQLKLHQQQF FIGKGQDQGR LWQIPLNANY
DAAPQIMKDQ DISLGEYQEL RDKVGKPFRL NLGNNSHFIV KYDETLLNDI LDHLDNLDAI
SQRQLLQDCR LLADGGEMSY ADLVPLLPKF ANSHSEIVNT ALYAIVNRLK LFVQPKSKEE
DQLKRLVDQL AAPQVARLGW QPSKDDSNDD QLTRPIVLSA ALYADNKKAI EAAHRIFTNH
QSDLAHLNAD IRPLVLKAEM QHYGNPALFE QFIRDYQDTA DASYKSDLNS AITATKSPKL
ISQLITDFED STVIKPQDLR GWYRNVLANN DGQQAAWDWL RGEWDWLNKT VGGDMEFATY
ITVTANVFHT PARLQEFKEF FEPKVNTPGL TREIKMDISI VQSKVDLIAK EQDAVHQAIQ
AAIQ
//
