ID A0A1E8GQQ5_9LACT Unreviewed; 284 AA.
AC A0A1E8GQQ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN Name=map {ECO:0000256|HAMAP-Rule:MF_01974};
GN ORFNames=BG261_01440 {ECO:0000313|EMBL:OFI50564.1};
OS Floricoccus tropicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Floricoccus.
OX NCBI_TaxID=1859473 {ECO:0000313|EMBL:OFI50564.1, ECO:0000313|Proteomes:UP000178622};
RN [1] {ECO:0000313|Proteomes:UP000178622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF1 {ECO:0000313|Proteomes:UP000178622};
RA Chuah L.-O., Yap K.-P., Thong K.L., Liong M.T., Ahmad R., Rusul G.;
RT "Draft genome sequence of a novel species of the family Streptococcaceae
RT isolated from flowers.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-Rule:MF_01974}.
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|HAMAP-Rule:MF_01974,
CC ECO:0000256|RuleBase:RU003653};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974};
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. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000256|HAMAP-Rule:MF_01974};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01974}.
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:OFI50564.1}.
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DR EMBL; MKIR01000001; OFI50564.1; -; Genomic_DNA.
DR RefSeq; WP_070791402.1; NZ_MKIR01000001.1.
DR AlphaFoldDB; A0A1E8GQQ5; -.
DR STRING; 1859473.BG261_01440; -.
DR OrthoDB; 9802055at2; -.
DR Proteomes; UP000178622; Unassembled WGS sequence.
DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR HAMAP; MF_01974; MetAP_1; 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:SF17; METHIONINE AMINOPEPTIDASE; 1.
DR Pfam; PF00557; Peptidase_M24; 2.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW ECO:0000256|RuleBase:RU003653};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974,
KW ECO:0000256|RuleBase:RU003653};
KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
KW Reference proteome {ECO:0000313|Proteomes:UP000178622}.
FT DOMAIN 11..100
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 129..269
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 197
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
SQ SEQUENCE 284 AA; 31687 MW; 285413A1A9C30514 CRC64;
MISLKSPREI EQMDKAGDFL ASIHIGLRDI IKPGIDMWDI EEYVRKRCKE ENFLPLQIGV
DGEIQDYPYA TCCSLNDEVA HAFPRHQTLK DGDLIKVDMV LGMASDDLDV SKLDFNNVQD
MKKYTESFRG GIADSCWAYA VGTPSEEVKN LMDVTKESLY RGIEQARVGN RMGDIGSAIQ
EYAEAHGYGV VRDLVGHGVG PTMHEEPMVP HYGVKGKGLR LREGMVLTIE PMINTGTYEI
DTDFKTGWAH KTLDGGLSCQ YEHQFVITKD GPVILTSQGE EGTY
//
