APEB_MYCLE
ID APEB_MYCLE Reviewed; 426 AA.
AC Q50022; O08111;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable M18 family aminopeptidase 2;
DE EC=3.4.11.-;
GN Name=apeB; Synonyms=pepC, pepX; OrderedLocusNames=ML2213;
GN ORFNames=MLCB5.29;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB08404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC31168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U15182; AAA62998.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z95151; CAB08404.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583924; CAC31168.1; ALT_INIT; Genomic_DNA.
DR PIR; H87185; H87185.
DR AlphaFoldDB; Q50022; -.
DR SMR; Q50022; -.
DR EnsemblBacteria; CAC31168; CAC31168; CAC31168.
DR KEGG; mle:ML2213; -.
DR Leproma; ML2213; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_019532_2_0_11; -.
DR Proteomes; UP000000806; Chromosome.
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 Gene3D; 2.30.250.10; -; 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; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..426
FT /note="Probable M18 family aminopeptidase 2"
FT /id="PRO_0000173463"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 45594 MW; 582ADDD29C3A0A53 CRC64;
MPASAADLCE FINASPSPFH VCATVAGRLL DAGYAELSEV ERWPDHPGRY FIVRAGSLVA
WSAGQGVKAH APFRIVGAHT DSPNLRVKQH PDLLVAGWRV VALQPYGGAW LNSWLDRDLG
VSGRLSVRSA GKGSEITDRL VRIDDPILRV PQLAIHLAED RKSLTLDPQR HVNAVWGVGD
KAGSLLEYVA ERTGVAVADV LAVDLMTHDL VPSMVIGADA NLLSAPRLDN QVSCYAGMEA
LLASVPHDCL PVLALFDHEE VGSTSDRGAR SNLLSTVLER IVLAAGGGRD DYLRRLPASL
LVSADMAHAT HPNYPECHEP SHLIEVNAGP VLKVHPNLRY ATDGRTAAAF EVACQQAGVR
LQRYEHRADR PCGSTIGPLA SARTGIPTVD VGAAQLAMHS ARELMGAHDV AVYSAALQAF
FSADLF