MAP11_MYCTU
ID MAP11_MYCTU Reviewed; 266 AA.
AC P9WK21; L0T6B7; Q79FX0; Q7D9D5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_01974};
DE Short=MAP 1 {ECO:0000255|HAMAP-Rule:MF_01974};
DE Short=MetAP 1 {ECO:0000255|HAMAP-Rule:MF_01974};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974};
GN Name=map-1 {ECO:0000255|HAMAP-Rule:MF_01974}; Synonyms=mapA;
GN OrderedLocusNames=Rv0734;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A METHIONINE AMINOPEPTIDASE, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND MASS SPECTROMETRY.
RX PubMed=19688379; DOI=10.1007/s00284-009-9470-3;
RA Zhang X., Chen S., Hu Z., Zhang L., Wang H.;
RT "Expression and characterization of two functional methionine
RT aminopeptidases from Mycobacterium tuberculosis H37Rv.";
RL Curr. Microbiol. 59:520-525(2009).
RN [3]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=20363127; DOI=10.1016/j.bmcl.2010.03.067;
RA Lu J.P., Ye Q.Z.;
RT "Expression and characterization of Mycobacterium tuberculosis methionine
RT aminopeptidase type 1a.";
RL Bioorg. Med. Chem. Lett. 20:2776-2779(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01974, ECO:0000269|PubMed:19688379}.
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:0000255|HAMAP-Rule:MF_01974};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01974};
CC -!- ACTIVITY REGULATION: Inhibited by various metalloform-selective
CC inhibitors. {ECO:0000269|PubMed:20363127}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20363127};
CC KM=328 uM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20363127};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. It retained half of its
CC activity after 10 min of incubation at 55 degrees Celsius.
CC {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20363127};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.
CC -!- MASS SPECTROMETRY: Mass=28812; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19688379};
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}.
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; AL123456; CCP43479.1; -; Genomic_DNA.
DR RefSeq; WP_003403728.1; NZ_NVQJ01000007.1.
DR RefSeq; YP_177748.1; NC_000962.3.
DR AlphaFoldDB; P9WK21; -.
DR SMR; P9WK21; -.
DR STRING; 83332.Rv0734; -.
DR PaxDb; P9WK21; -.
DR PRIDE; P9WK21; -.
DR DNASU; 888564; -.
DR GeneID; 45424699; -.
DR GeneID; 888564; -.
DR KEGG; mtu:Rv0734; -.
DR TubercuList; Rv0734; -.
DR eggNOG; COG0024; Bacteria.
DR OMA; HWEHSVA; -.
DR PhylomeDB; P9WK21; -.
DR BRENDA; 3.4.11.18; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0050897; F:cobalt ion binding; IDA:MTBBASE.
DR GO; GO:0005506; F:iron ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:MTBBASE.
DR GO; GO:0016151; F:nickel cation binding; IDA:MTBBASE.
DR GO; GO:0006555; P:methionine metabolic process; IDA:MTBBASE.
DR GO; GO:0070084; P:protein initiator methionine removal; IBA:GO_Central.
DR GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IDA:MTBBASE.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 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 Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Hydrolase; Metal-binding; Protease; Reference proteome.
FT CHAIN 1..266
FT /note="Methionine aminopeptidase 1"
FT /id="PRO_0000414588"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 117
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 117
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 186
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
SQ SEQUENCE 266 AA; 27277 MW; A187BD61E62449E1 CRC64;
MRPLARLRGR RVVPQRSAGE LDAMAAAGAV VAAALRAIRA AAAPGTSSLS LDEIAESVIR
ESGATPSFLG YHGYPASICA SINDRVVHGI PSTAEVLAPG DLVSIDCGAV LDGWHGDAAI
TFGVGALSDA DEALSEATRE SLQAGIAAMV VGNRLTDVAH AIETGTRAAE LRYGRSFGIV
AGYGGHGIGR QMHMDPFLPN EGAPGRGPLL AAGSVLAIEP MLTLGTTKTV VLDDKWTVTT
ADGSRAAHWE HTVAVTDDGP RILTLG
