ID A0A1A1WBL6_9MYCO Unreviewed; 420 AA.
AC A0A1A1WBL6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN ORFNames=A5730_19030 {ECO:0000313|EMBL:OBF04233.1};
OS Mycobacterium sp. ACS4054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834119 {ECO:0000313|EMBL:OBF04233.1, ECO:0000313|Proteomes:UP000091876};
RN [1] {ECO:0000313|EMBL:OBF04233.1, ECO:0000313|Proteomes:UP000091876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS4054 {ECO:0000313|EMBL:OBF04233.1,
RC ECO:0000313|Proteomes:UP000091876};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467,
CC ECO:0000256|RuleBase:RU004386}.
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:OBF04233.1}.
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DR EMBL; LZHV01000061; OBF04233.1; -; Genomic_DNA.
DR RefSeq; WP_067904444.1; NZ_LZHV01000061.1.
DR AlphaFoldDB; A0A1A1WBL6; -.
DR STRING; 1834119.A5730_19030; -.
DR OrthoDB; 5288740at2; -.
DR Proteomes; UP000091876; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR InterPro; IPR022984; M18_aminopeptidase_2.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
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, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_00467};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}.
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467"
SQ SEQUENCE 420 AA; 44489 MW; A79DC9303B087ACB CRC64;
MSASAAGLCD FIDASPSPFH VCATVAARLT AAGYTELSEA KRWPEEPGRY FTVRAGSLVA
WNSEGADGPF RIVGAHTDSP NLRVKQHPDR VVAGWRVVAL EPYGGAWLNS WLDRDLGISG
RLSLRAGAGI EHRLVRIDEP ILRVPQLAIH LAEDRKSLTL DPQRHVNAVW GVGADAKSFV
DYVAERAGVD PTGVLAADLM THDLTPSTVV GAGADLLSAP RLDNQASCYA GMEALLAAGP
RGFLPVLVLF DHEEVGSSSD HGAQSDLLGT VLERIVLAAG GTREDFLRRL PDSLLASADM
AHATHPNYPE RHEPGHLIEA NAGPVLKVHP NLRYATDGRT AAAFALACQQ AGVALQRYEH
RADLPCGSTI GPLASARTGI PTVDVGAAQL AMHSARELMG AEDVAAYAAA MRAFLSPEPS
//
