ID A0A271UD45_ECOLX Unreviewed; 265 AA. AC A0A271UD45; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 02-OCT-2024, entry version 34. DE RecName: Full=Mlc titration factor A {ECO:0000256|HAMAP-Rule:MF_01593}; DE AltName: Full=Probable zinc metallopeptidase MtfA {ECO:0000256|HAMAP-Rule:MF_01593}; DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_01593}; GN Name=mtfA {ECO:0000256|HAMAP-Rule:MF_01593, GN ECO:0000313|EMBL:EFM1447388.1}; GN ORFNames=FKO60_01190 {ECO:0000313|EMBL:TZE52271.1}, HEP34_003772 GN {ECO:0000313|EMBL:EFM1447388.1}, TUM18780_17010 GN {ECO:0000313|EMBL:BCG36539.1}; OS Escherichia coli. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:EFM1447388.1, ECO:0000313|Proteomes:UP000519182}; RN [1] {ECO:0000313|EMBL:TZE52271.1, ECO:0000313|Proteomes:UP000324120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=347 {ECO:0000313|EMBL:TZE52271.1, RC ECO:0000313|Proteomes:UP000324120}; RA Cormier A.C., Chalmer G., Cook S.R., Zaheer R., Hannon S.J., Booker C.W., RA Read R., Gow S.P., Mcallister T.A., Boerlin P.; RT "The presence and diversity of blaCTX-M among Escherichia coli from urban RT wastewater and feedlot cattle, in Alberta, Canada."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFM1447388.1, ECO:0000313|Proteomes:UP000519182} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PSU-2464 {ECO:0000313|EMBL:EFM1447388.1, RC ECO:0000313|Proteomes:UP000519182}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BCG36539.1, ECO:0000313|Proteomes:UP000509260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TUM18780 {ECO:0000313|EMBL:BCG36539.1, RC ECO:0000313|Proteomes:UP000509260}; RA Ito Y., Aoki K., Nakayama N., Ohtsuka M., Ota M., Kaneko N., Yoshida M., RA Ishii Y., Tateda K., Matsuse H.; RT "Whole-genome sequencing of blaNDM-5 positive Escherichia coli isolated RT from a Japanese patient with no history of travel abroad."; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the modulation of the activity of the glucose- CC phosphotransferase system (glucose-PTS). Interacts with the CC transcriptional repressor Mlc, preventing its interaction with DNA and CC leading to the modulation of expression of genes regulated by Mlc, CC including ptsG, which encodes the PTS system glucose-specific EIICB CC component. {ECO:0000256|HAMAP-Rule:MF_01593}. CC -!- FUNCTION: Shows zinc-dependent metallopeptidase activity. CC {ECO:0000256|HAMAP-Rule:MF_01593}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01593}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01593}; CC -!- SUBUNIT: Interacts with Mlc. {ECO:0000256|HAMAP-Rule:MF_01593}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01593}. CC -!- SIMILARITY: Belongs to the MtfA family. {ECO:0000256|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; AP023197; BCG36539.1; -; Genomic_DNA. DR EMBL; AATJYL010000038; EFM1447388.1; -; Genomic_DNA. DR EMBL; VHKY01000001; TZE52271.1; -; Genomic_DNA. DR RefSeq; WP_001362605.1; NZ_WTSM01000001.1. DR Proteomes; UP000324120; Unassembled WGS sequence. DR Proteomes; UP000509260; Chromosome. DR Proteomes; UP000519182; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd20169; Peptidase_M90_mtfA; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR Gene3D; 1.10.472.150; Glucose-regulated metallo-peptidase M90, N-terminal domain; 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; MTFA PEPTIDASE; 1. DR PANTHER; PTHR30164:SF2; PROTEIN MTFA; 1. DR Pfam; PF06167; Peptidase_M90; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_01593}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01593}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01593}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01593}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_01593}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01593}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01593}. FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01593" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01593" FT BINDING 152 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01593" FT BINDING 211 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01593" SQ SEQUENCE 265 AA; 30309 MW; 198E36659BBCF8A5 CRC64; MIKWPWKVQE SAHQTALPWQ EALSIPLLTC LTEQEQSKLV TLAERFLQQK RLVPLQGFEL DSLRSCRIAL LFCLPVLELG LEWLDGFHEV LIYPAPFVVD DEWEDDIGLV HNQRIVQSGQ SWQQGPIVLN WLDIQDSFDA SGFNLIIHEV AHKLDTRNGD RASGVPFIPL REVAGWEHDL HAAMNNIQEE IELVGENAAS IDAYAASDPA ECFAVLSEYF FSAPELFAPR FPSLWQRFCQ FYQQDPLQRL HHANDTDSFS TTNVH //