ID U6F3W8_LACHE Unreviewed; 360 AA.
AC U6F3W8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Peptidase M42 family {ECO:0000313|EMBL:CDI58631.1};
GN ORFNames=LHCIRMBIA951_00691 {ECO:0000313|EMBL:CDI58631.1};
OS Lactobacillus helveticus CIRM-BIA 951.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1226334 {ECO:0000313|EMBL:CDI58631.1, ECO:0000313|Proteomes:UP000017248};
RN [1] {ECO:0000313|EMBL:CDI58631.1, ECO:0000313|Proteomes:UP000017248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRM-BIA 951 {ECO:0000313|EMBL:CDI58631.1,
RC ECO:0000313|Proteomes:UP000017248};
RA Valence F., Chuat V., Ma L., Creno S., Falentin H., Lortal S., Bizet C.,
RA Clermont D., Loux V., Bouchier C., Cousin S.;
RT "Draft Genome Sequence of five Lactobacillus helveticus strains CIRM-BIA
RT 101T, 103, 104, 951 and 953 isolated from milk product.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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:CDI58631.1}.
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DR EMBL; CBUK010000085; CDI58631.1; -; Genomic_DNA.
DR RefSeq; WP_003633113.1; NZ_HG530839.1.
DR AlphaFoldDB; U6F3W8; -.
DR HOGENOM; CLU_047249_0_2_9; -.
DR Proteomes; UP000017248; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000017248}.
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 360 AA; 40080 MW; E23A8E2745EB729B CRC64;
MQKEQEIQML KEFSDANSTS GFEEEFVKLF TSYAEKTANI EVDGMLNVYA SKKENKGDRP
VIQLDAHSDA VGFITQAVRP NGLIKFVPLG GWVKYNIPAL KVKVRNRDGE YIPGVVATKP
PHFMTAAERN NVPDVVDMSI DVGSSSREET IKDYKIDTGC PIFVDVKCEY HEKSGLFFGK
DFDDRFGAGA MIDVLDNLKG EETNFDVVAA LSSQEEVGLR GAYVTARKVK PDLCLVLESC
PADDTFTPDW LSQTGLKRGP MLRDMDTTFL PNPKFQQYAC DLADKNNIPY TRSVRTGGGQ
DGAAIYYENG APTIVIGIPV RYEHSPYCFS SYKDFKASVD LATAIIRDIT QEKLDSFKKF
//
