ID   MTFA_PECCP              Reviewed;         265 AA.
AC   C6DDR1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-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}; OrderedLocusNames=PC1_1479;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT12523.1; -; Genomic_DNA.
DR   RefSeq; WP_015839749.1; NC_012917.1.
DR   AlphaFoldDB; C6DDR1; -.
DR   SMR; C6DDR1; -.
DR   STRING; 561230.PC1_1479; -.
DR   MEROPS; M90.001; -.
DR   EnsemblBacteria; ACT12523; ACT12523; PC1_1479.
DR   KEGG; pct:PC1_1479; -.
DR   eggNOG; COG3228; Bacteria.
DR   HOGENOM; CLU_063037_2_0_6; -.
DR   OMA; EHSGEAW; -.
DR   OrthoDB; 1806453at2; -.
DR   Proteomes; UP000002736; 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_1000215652"
SQ   SEQUENCE   265 AA;  30336 MW;  53846D6A111507C5 CRC64;
     MIKWPWKNSQ PQVQTLEHWQ AAISIPLLAP LSDEERQKLV TLADQFLKQK RLIPLQELVL
     TEIMQQRIAL LFSLPVLSLG IDALDGFHEV LVYPGPFIVE EEWQDDIGLV HTGKMVQSGQ
     SWDQGPIVLN WQEVQDSFDL SGFNLIIHEV AHKLDIRSSG EATGVPLIPL RDIAVWEQHL
     HGAMDALQEE IDLVGEEAAS MDPYAVHDPA ECFAVLSEYF FSAPELLDER FPDLYRCFQK
     FYRQDPLARL KSWQSSVNYR APSIY