ID X8CPB5_MYCIT Unreviewed; 377 AA.
AC X8CPB5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=M42 glutamyl aminopeptidase family protein {ECO:0000313|EMBL:EUA57701.1};
GN ORFNames=I550_0829 {ECO:0000313|EMBL:EUA57701.1};
OS Mycobacterium intracellulare 1956.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1299331 {ECO:0000313|EMBL:EUA57701.1, ECO:0000313|Proteomes:UP000020825};
RN [1] {ECO:0000313|EMBL:EUA57701.1, ECO:0000313|Proteomes:UP000020825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1956 {ECO:0000313|EMBL:EUA57701.1,
RC ECO:0000313|Proteomes:UP000020825};
RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (DEC-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:EUA57701.1}.
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DR EMBL; JAOG01000001; EUA57701.1; -; Genomic_DNA.
DR AlphaFoldDB; X8CPB5; -.
DR PATRIC; fig|1299331.3.peg.809; -.
DR Proteomes; UP000020825; 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 ECO:0000313|EMBL:EUA57701.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 377 AA; 40437 MW; F4B998A887675DA1 CRC64;
MAHPDRDAGD DLLQELLWTY GPCGQEDEVR AVIARELQPL VDDMWTDDAG NLIGYVAANA
SAKNTGAPDH RQRTQAIPGT ATRVMAHMDE LSMIVKRVES DGTLHLTQLG TMYPGNFGLG
PVAVLGDNET LTAVLALGSE HTTQESSRIW ETKPDKGDRA LDWHHVYVFT GRSTEELAAA
GVHAGTRVCV DRSKRSVVEI GDYVGAYFLD DRAAVTALLN AARLLRERNQ RPADDVYLVF
TTNEEIGGVG GTYASATLPG HLTLALEVGP TEVEYNTTVS GGPIIGYSDA LCIYDKEIAD
RLLKIATDQG LSPQPAALGA FESDASHAKA TGQAARAGLL CLPTLSTHGY EVIARRAIDD
MAAIIVDFVL QPSQQIA
//