ID A0A0G0KS35_9BACT Unreviewed; 253 AA.
AC A0A0G0KS35;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 29.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|RuleBase:RU003653};
DE EC=3.4.11.18 {ECO:0000256|RuleBase:RU003653};
GN ORFNames=US72_C0011G0038 {ECO:0000313|EMBL:KKQ51939.1};
OS Microgenomates group bacterium GW2011_GWC1_38_12.
OC Bacteria.
OX NCBI_TaxID=1618512 {ECO:0000313|EMBL:KKQ51939.1, ECO:0000313|Proteomes:UP000034948};
RN [1] {ECO:0000313|EMBL:KKQ51939.1, ECO:0000313|Proteomes:UP000034948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC N-terminal methionine is often cleaved when the second residue in the
CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC Thr, or Val). Requires deformylation of the N(alpha)-formylated
CC initiator methionine before it can be hydrolyzed.
CC {ECO:0000256|ARBA:ARBA00002521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU003653};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions.
CC {ECO:0000256|RuleBase:RU003653};
CC -!- SIMILARITY: Belongs to the peptidase M24A family.
CC {ECO:0000256|RuleBase:RU003653}.
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:KKQ51939.1}.
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DR EMBL; LBUB01000011; KKQ51939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0KS35; -.
DR PATRIC; fig|1618512.3.peg.788; -.
DR Proteomes; UP000034948; Unassembled WGS sequence.
DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR NCBIfam; TIGR00500; met_pdase_I; 1.
DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43330:SF8; METHIONINE AMINOPEPTIDASE 1D, MITOCHONDRIAL; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU003653,
KW ECO:0000313|EMBL:KKQ51939.1}; Hydrolase {ECO:0000313|EMBL:KKQ51939.1};
KW Metal-binding {ECO:0000256|RuleBase:RU003653};
KW Protease {ECO:0000256|RuleBase:RU003653}.
FT DOMAIN 17..245
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 253 AA; 27585 MW; D9CC67C5A0F29EC8 CRC64;
MRENTKIPIK TPDEIEVMRE GGRKLVKVKK ELLEAVKEGV RASEIDNLAD KLIEKEGGEA
SFKMVSGYSW ATCVNINEGV VHGIPKKEIV FKRNDVVSVD VGMFYKGFHT DTSFTKAIGS
NPNLERFLGS GRSALEKAIQ EARIGNRIYD ISQAIESTMR KNGYSPIRAL VGHGVGRALH
EEPQVPCFTN GNREESPEIP LGAVFAVEVM YAMGSPDVKI ASDGWTISTS DGTISGLFED
TVVVSPKGPL VIT
//
