ID A0A0F2E0S9_STROR Unreviewed; 286 AA.
AC A0A0F2E0S9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974};
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};
DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN Name=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN ECO:0000313|EMBL:KJQ76903.1};
GN ORFNames=TZ95_00750 {ECO:0000313|EMBL:KJQ76903.1};
OS Streptococcus oralis subsp. tigurinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1077464 {ECO:0000313|EMBL:KJQ76903.1, ECO:0000313|Proteomes:UP000033377};
RN [1] {ECO:0000313|EMBL:KJQ76903.1, ECO:0000313|Proteomes:UP000033377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC5873 {ECO:0000313|EMBL:KJQ76903.1,
RC ECO:0000313|Proteomes:UP000033377};
RA Haase E.M.;
RT "Evolution of amylase-binding proteins of oral streptococcal species.";
RL Submitted (FEB-2015) 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 -!- 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:KJQ76903.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYGU01000006; KJQ76903.1; -; Genomic_DNA.
DR RefSeq; WP_045617004.1; NZ_JYGU01000006.1.
DR AlphaFoldDB; A0A0F2E0S9; -.
DR PATRIC; fig|28037.217.peg.722; -.
DR OrthoDB; 9802055at2; -.
DR Proteomes; UP000033377; Unassembled WGS sequence.
DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
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; 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 SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW ECO:0000313|EMBL:KJQ76903.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000313|EMBL:KJQ76903.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974};
KW Protease {ECO:0000256|HAMAP-Rule:MF_01974}.
FT DOMAIN 11..99
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 129..271
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 136
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 136
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 199
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 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT BINDING 232
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 264
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 264
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 286 AA; 31617 MW; 6C62BA57FC4FD52E CRC64;
MITLKSAREI EAMNKAGDFL ASIHIGLRDL IKPGVDMWEV EEYVRRRCKE ENFLPLQIGV
DGAVMDYPYA TCCSLNDEVA HAFPRHYILK DGDLLKVDMV LGGPIAKSDL NVSKLNFNNV
EQMKKYTQSY TGGLADSCWA YAVGTPSEEV KNLMDVTKEA MYKGIEQAVV GNRIGDIGAA
IQEYAESRGY GVVRDLVGHG VGPTMHEEPM VPNYGVAGRG LRLREGMVLT IEPMINTGDW
EIDTDMKTGW AHKTIDGGLS CQYEHQFVIT KDGPVILTSQ GEEGTY
//
