ID   MFTE_MYCTO              Reviewed;         251 AA.
AC   P9WP58; L0T678; P95041; Q7D9E8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Mycofactocin precursor peptide peptidase;
DE            EC=3.4.14.- {ECO:0000250|UniProtKB:A0PM51};
GN   Name=mftE; OrderedLocusNames=MT0722;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Peptidase involved in the biosynthesis of the enzyme cofactor
CC       mycofactocin (MFT). Catalyzes cleavage of the MftC-modified MftA
CC       peptide to liberate its final two residues, which consist of a cross-
CC       linked valine-decarboxylated tyrosine dipeptide (named 3-amino-5-[(4-
CC       hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one or ADHP).
CC       {ECO:0000250|UniProtKB:A0PM51}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[mycofactocin precursor peptide]-C-terminal glycyl-N-{5-[(4-
CC         hydroxyphenyl)methyl]-4,4-dimethyl-2-oxopyrrolidin-3-yl}acetamide +
CC         H2O = 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-
CC         2-one + [mycofactocin precursor peptide]-C-terminal glycine;
CC         Xref=Rhea:RHEA:65504, Rhea:RHEA-COMP:16818, Rhea:RHEA-COMP:16819,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:83148, ChEBI:CHEBI:150863,
CC         ChEBI:CHEBI:156518; Evidence={ECO:0000250|UniProtKB:A0PM51};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:A0PM51};
CC       Note=MftE appears to bind one Fe(2+) and one Zn(2+) ion per subunit.
CC       Fe(2+) seems to be catalytically active while Zn(2+) could play an
CC       auxiliary role. {ECO:0000250|UniProtKB:A0PM51};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:A0PM51};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:A0PM51}.
CC   -!- SIMILARITY: Belongs to the creatininase superfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44951.1; -; Genomic_DNA.
DR   PIR; B70641; B70641.
DR   RefSeq; WP_003403497.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP58; -.
DR   SMR; P9WP58; -.
DR   EnsemblBacteria; AAK44951; AAK44951; MT0722.
DR   GeneID; 45424659; -.
DR   KEGG; mtc:MT0722; -.
DR   PATRIC; fig|83331.31.peg.772; -.
DR   HOGENOM; CLU_055029_4_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10310; -; 1.
DR   InterPro; IPR024087; Creatininase-like_sf.
DR   InterPro; IPR003785; Creatininase/forma_Hydrolase.
DR   InterPro; IPR023871; MftE.
DR   PANTHER; PTHR35005; PTHR35005; 1.
DR   Pfam; PF02633; Creatininase; 1.
DR   SUPFAM; SSF102215; SSF102215; 1.
DR   TIGRFAMs; TIGR03964; mycofact_creat; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Zinc.
FT   CHAIN           1..251
FT                   /note="Mycofactocin precursor peptide peptidase"
FT                   /id="PRO_0000427009"
FT   BINDING         38
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P83772"
FT   BINDING         40
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P83772"
FT   BINDING         49
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P83772"
FT   BINDING         49
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P83772"
FT   BINDING         128
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P83772"
FT   BINDING         167
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P83772"
SQ   SEQUENCE   251 AA;  26580 MW;  6C0882C57D15EAF0 CRC64;
     MNSSYHRRVP VVGELGSATS SQLPSTSPSI VIPLGSTEQH GPHLPLDTDT RIATAVARTV
     TARLHAEDLP IAQEEWLMAP AIAYGASGEH QRFAGTISIG TEALTMLLVE YGRSAACWAR
     RLVFVNGHGG NVGALTRAVG LLRAEGRDAG WCPCTCPGGD PHAGHTETSV LLHLSPADVR
     TERWRAGNRA PLPVLLPSMR RGGVAAVSET GVLGDPTTAT AAEGRRIFAA MVDDCVRRVA
     RWMPQPDGML T