ID   MTFA_ECOL5              Reviewed;         265 AA.
AC   Q0TGJ4; Q7BQS3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=ECP_1934;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10518744; DOI=10.1111/j.1574-6968.1999.tb08756.x;
RA   Schubert S., Rakin A., Fischer D., Sorsa J., Heesemann J.;
RT   "Characterization of the integration site of Yersinia high-pathogenicity
RT   island in Escherichia coli.";
RL   FEMS Microbiol. Lett. 179:409-414(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; AF135406; AAD37508.1; -; Genomic_DNA.
DR   EMBL; CP000247; ABG69935.1; -; Genomic_DNA.
DR   RefSeq; WP_001325918.1; NC_008253.1.
DR   AlphaFoldDB; Q0TGJ4; -.
DR   SMR; Q0TGJ4; -.
DR   STRING; 362663.ECP_1934; -.
DR   MEROPS; M90.001; -.
DR   EnsemblBacteria; ABG69935; ABG69935; ECP_1934.
DR   KEGG; ecp:ECP_1934; -.
DR   HOGENOM; CLU_063037_2_0_6; -.
DR   OMA; EHSGEAW; -.
DR   Proteomes; UP000009182; 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_0000316315"
FT   CONFLICT        41
FT                   /note="A -> T (in Ref. 1; AAD37508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="N -> D (in Ref. 1; AAD37508)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="S -> P (in Ref. 1; AAD37508)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  30238 MW;  ABB033E86773BC10 CRC64;
     MIKWPWKVQE SAHQTALPWQ EALSIPLLTC LTEQEQSKLV ALAERFLQQK RLVPLQGFEL
     NSLRSCRIAL LFCLPVLELG LEWLDGFHEV LIYPAPFVVD DEWEDDIGLV HNQRIVQSGQ
     SWQQGPIVLN WLDIQDSFDA SGFNLIIHEV AHKLDTRNGD RASGVPFISL REVAGWEHDL
     HAAMNNIQEE IELVGENAAS IDAYAASDPA ECFAVLSEYF FSAPELFAPR FPSLWQRFCQ
     FYQQDPLQRL HHANDTDSFS ATNVH