MTFA_YERPS
ID MTFA_YERPS Reviewed; 270 AA.
AC Q66C05; Q9ZEX5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=YPTB1611;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-270.
RC STRAIN=IP32637 / Serotype I;
RX PubMed=9988474; DOI=10.1046/j.1365-2958.1998.01124.x;
RA Buchrieser C., Brosch R., Bach S., Guiyoule A., Carniel E.;
RT "The high-pathogenicity island of Yersinia pseudotuberculosis can be
RT inserted into any of the three chromosomal asn tRNA genes.";
RL Mol. Microbiol. 30:965-978(1998).
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; BX936398; CAH20850.1; -; Genomic_DNA.
DR EMBL; AJ009592; CAA08753.1; -; Genomic_DNA.
DR RefSeq; WP_002211042.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66C05; -.
DR SMR; Q66C05; -.
DR MEROPS; M90.001; -.
DR EnsemblBacteria; CAH20850; CAH20850; YPTB1611.
DR GeneID; 66841955; -.
DR KEGG; ypo:BZ17_893; -.
DR KEGG; yps:YPTB1611; -.
DR PATRIC; fig|273123.14.peg.950; -.
DR OMA; EHSGEAW; -.
DR Proteomes; UP000001011; 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..270
FT /note="Protein MtfA"
FT /id="PRO_0000316333"
FT CONFLICT 190
FT /note="E -> K (in Ref. 2; CAA08753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 30659 MW; 954F314F6E3F14CE CRC64;
MIKWLWKANK PQAEMLAQWH EALNIPLLAP LNEPEQQRLV SVASQLLQQK RFIPLQGLIL
TPLMQARLAL LFALPVMELG AKWLDGFHEV LIYPSPFIVA EDWQDDLGLV HSGQSVQSGQ
SWEQGPIVLN WQDIQDSFDL SGFNLVIHEA AHKLDMRNGG HSNGVPPIAM RDVAVWEHDL
HHAMDNIQDE IDMVGVEGAS MDAYAASNPA ECFAVLSEYF FSAPELLEGR FPAVYQHFCR
FYRQDPLARL KRWENSLADN PPPENTHSHR