ID A0A1E3TLL4_MYCSH Unreviewed; 361 AA.
AC A0A1E3TLL4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase M42 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MSP7336_01020 {ECO:0000313|EMBL:SRX92794.1};
OS Mycobacterium shimoidei.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29313 {ECO:0000313|EMBL:SRX92794.1, ECO:0000313|Proteomes:UP000252015};
RN [1] {ECO:0000313|EMBL:SRX92794.1, ECO:0000313|Proteomes:UP000252015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7336 {ECO:0000313|EMBL:SRX92794.1,
RC ECO:0000313|Proteomes:UP000252015};
RG IHU Genomes;
RL Submitted (MAY-2018) 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}.
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DR EMBL; UEGW01000001; SRX92794.1; -; Genomic_DNA.
DR RefSeq; WP_069394129.1; NZ_UEGW01000001.1.
DR AlphaFoldDB; A0A1E3TLL4; -.
DR STRING; 29313.BHQ16_01030; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000252015; 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}.
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 361 AA; 38583 MW; D1B9BEAF62BA3C59 CRC64;
MAQRDHDSGD DLLQELLLAY GPCGQEDAVR ELCARELQPV VDDMWTDEAG NLIGHLRATD
GAGDDAATRL MAHMDELSMM VKRIGSDGTL HLTQLGTMYP GNFGLGPVAV LGDHQTFTAV
LTLGSEHTTK ESPKIWETKP DQGDKALDWQ HVYVFTGRTA EELTAAGVHP GTRVCVDRSK
RTLVELGDYL GSYFLDDRAA VTALLRAARL LREREQRPAE DVYFVFTTNE EIGGVGGSYA
SASLPGRLTL ALEVGPTEQE YGTSVTGGPI IGYSDAQCVY DKDVADRLMA IATERGLAPQ
AAALGAFESD ASHAKASGLT PCAGLLCLPT LSTHGFEVIA RSAIDAMAAI VVDFLLPSRA
S
//