ID   MTFA_ECOK1              Reviewed;         265 AA.
AC   A1ACG4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Protein MtfA {ECO:0000255|HAMAP-Rule:MF_01593};
DE   AltName: Full=Mlc titration factor A {ECO:0000255|HAMAP-Rule:MF_01593};
GN   Name=mtfA {ECO:0000255|HAMAP-Rule:MF_01593}; OrderedLocusNames=Ecok1_18600;
GN   ORFNames=APECO1_1050;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- FUNCTION: Involved in the regulation of ptsG expression by binding and
CC       inactivating Mlc. {ECO:0000255|HAMAP-Rule:MF_01593}.
CC   -!- SUBUNIT: Interacts with Mlc. {ECO:0000255|HAMAP-Rule:MF_01593}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01593}.
CC   -!- SIMILARITY: Belongs to the MtfA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01593}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ01354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ01354.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001350677.1; NC_008563.1.
DR   AlphaFoldDB; A1ACG4; -.
DR   SMR; A1ACG4; -.
DR   MEROPS; M90.001; -.
DR   EnsemblBacteria; ABJ01354; ABJ01354; APECO1_1050.
DR   KEGG; ecv:APECO1_1050; -.
DR   HOGENOM; CLU_063037_0_1_6; -.
DR   Proteomes; UP000008216; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR   CDD; cd20169; Peptidase_M90_mtfA; 1.
DR   Gene3D; 1.10.472.150; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   HAMAP; MF_01593; MtfA; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR010384; MtfA_fam.
DR   InterPro; IPR042252; MtfA_N.
DR   PANTHER; PTHR30164; PTHR30164; 1.
DR   Pfam; PF06167; Peptidase_M90; 1.
PE   3: Inferred from homology;
KW   Cytoplasm.
FT   CHAIN           1..265
FT                   /note="Protein MtfA"
FT                   /id="PRO_0000316313"
SQ   SEQUENCE   265 AA;  30308 MW;  50E4850799BF2B68 CRC64;
     MIKWPWKVQE SAHQTALPWQ EALSIPLLTC LTEQEQSKLV TLAERFLQQK RLVPLQGFEL
     NSLRSCRIAL LFCLPVLELG LEWLDSFHEV LIYPAPFVVD DEWEDDIGLV HNQRIVQSGQ
     SWQQGPIVLN WLDIQDSFDA SGFNLIIHEV AHKLDTRNGD RASGVPFIPL REVAGWEHDL
     HAAMNNIQEE IELVGENAAS IDAYAASDPA ECFAVLSEYF FSAPELFAPR FPSLWQRFCQ
     FYQQDPLQRL HHANDTDSFS ATNVH