ID   MTFA_ECO7I              Reviewed;         265 AA.
AC   B7NRA8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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};
GN   OrderedLocusNames=ECIAI39_1082;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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}.
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DR   EMBL; CU928164; CAR17217.1; -; Genomic_DNA.
DR   RefSeq; WP_001311896.1; NC_011750.1.
DR   RefSeq; YP_002407095.1; NC_011750.1.
DR   AlphaFoldDB; B7NRA8; -.
DR   SMR; B7NRA8; -.
DR   STRING; 585057.ECIAI39_1082; -.
DR   MEROPS; M90.001; -.
DR   EnsemblBacteria; CAR17217; CAR17217; ECIAI39_1082.
DR   KEGG; ect:ECIAI39_1082; -.
DR   PATRIC; fig|585057.6.peg.1133; -.
DR   HOGENOM; CLU_063037_2_0_6; -.
DR   OMA; EHSGEAW; -.
DR   Proteomes; UP000000749; 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_1000147834"
SQ   SEQUENCE   265 AA;  30252 MW;  70D5864AC6B4B773 CRC64;
     MIKWPWKVQE SAHQTALPWQ EALSIPLLTC LTEQEQSKLV ALAERFLQQK RLVPLQGFEL
     NSLRSCRIAL LFCLPVLELG LEWLDGFHEI LIYPAPFVVD DEWEDDIGLV HNQRIVQSGQ
     SWQQGPIVLN WLDIQDSFDA SGFNLIIHEV AHKLDTRNGD RASGVPFISL REVAGWEHDL
     HAAMNNIQEE IELVGENAAS IDAYAASDPA ECFAVLSEYF FSAPELFAPR FPSLWQRFCQ
     FYQQDPLQRL HHANDTDSFS ATNVH