ID   MTFA_KLEP7              Reviewed;         265 AA.
AC   A6TB83;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 73.
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};
GN   OrderedLocusNames=KPN78578_23930; ORFNames=KPN_02432;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABR77854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000647; ABR77854.1; ALT_INIT; Genomic_DNA.
DR   PDB; 3DL1; X-ray; 2.20 A; A=1-265.
DR   PDB; 3KHI; X-ray; 1.95 A; A=1-265.
DR   PDBsum; 3DL1; -.
DR   PDBsum; 3KHI; -.
DR   AlphaFoldDB; A6TB83; -.
DR   SMR; A6TB83; -.
DR   STRING; 272620.KPN_02432; -.
DR   MEROPS; M90.001; -.
DR   EnsemblBacteria; ABR77854; ABR77854; KPN_02432.
DR   KEGG; kpn:KPN_02432; -.
DR   HOGENOM; CLU_063037_2_0_6; -.
DR   OMA; EHSGEAW; -.
DR   EvolutionaryTrace; A6TB83; -.
DR   Proteomes; UP000000265; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome.
FT   CHAIN           1..265
FT                   /note="Protein MtfA"
FT                   /id="PRO_0000316318"
FT   HELIX           19..23
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           33..49
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           62..73
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           109..115
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           131..137
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           145..155
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           173..194
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:3DL1"
FT   HELIX           203..206
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           209..222
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   TURN            228..230
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           232..242
FT                   /evidence="ECO:0007829|PDB:3KHI"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:3KHI"
SQ   SEQUENCE   265 AA;  30173 MW;  1777A63321F48216 CRC64;
     MFKWPWKADD ESGNAEMPWE QALAIPVLAH LSSTEQHKLT QMAARFLQQK RLVALQGLEL
     TPLHQARIAM LFCLPVLELG IEWLDGFHEV LIYPAPFIVD DEWEDDIGLV HNQRVVQSGQ
     SWQQGPVVLN WLDIQDSFDA SGFNLVVHEV AHKLDTRNGD RASGVPLIPL REVAGWEHDL
     HAAMNNIQDE IDLVGESAAS IDAYAATDPA ECFAVLSEYF FSAPELFAPR FPALWQRFCH
     FYRQDPLARR RENGLQDEGD RRIVH