ID   MTFA_ECOHS              Reviewed;         265 AA.
AC   A8A1J6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=EcHS_A2099;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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   ---------------------------------------------------------------------------
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; CP000802; ABV06400.1; -; Genomic_DNA.
DR   RefSeq; WP_001515476.1; NC_009800.1.
DR   AlphaFoldDB; A8A1J6; -.
DR   SMR; A8A1J6; -.
DR   MEROPS; M90.001; -.
DR   KEGG; ecx:EcHS_A2099; -.
DR   HOGENOM; CLU_063037_2_0_6; -.
DR   OMA; EHSGEAW; -.
DR   Proteomes; UP000001123; 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_0000316316"
SQ   SEQUENCE   265 AA;  30282 MW;  B438ED09615E6251 CRC64;
     MIKWPWKVQE SAHQTALPWQ EALSIPLLTG LTEQEQSKLV TLAERFLQQK RLVPLQGFEL
     DSLRSCRIAL LFCLPVLELG LEWLDGFHEV LIYPAPFVVD DEWEDDIGLV HNQRIVQSGQ
     SWQQGPIVLN WLDIQDSFDA SGFNLIIHEV AHKLDTRNGD RASGVPFIPL REVAGWEHDL
     HAAMNNIQEE IELVGENAAS IDAYAASDPA ECFAVLSEYF FSAPELFAPR FPSLWQRFCQ
     FYQQDPLQRL HRTNDTDSFS ATNVH