ID   YGFZ_ECO27              Reviewed;         326 AA.
AC   B7UHU7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   Name=ygfZ {ECO:0000255|HAMAP-Rule:MF_01175}; OrderedLocusNames=E2348C_3151;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Folate-binding protein involved in regulating the level of
CC       ATP-DnaA and in the modification of some tRNAs. It is probably a key
CC       factor in regulatory networks that act via tRNA modification, such as
CC       initiation of chromosomal replication. {ECO:0000255|HAMAP-
CC       Rule:MF_01175}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01175}.
CC   -!- SIMILARITY: Belongs to the tRNA-modifying YgfZ family.
CC       {ECO:0000255|HAMAP-Rule:MF_01175}.
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; FM180568; CAS10699.1; -; Genomic_DNA.
DR   RefSeq; WP_000886076.1; NC_011601.1.
DR   AlphaFoldDB; B7UHU7; -.
DR   SMR; B7UHU7; -.
DR   EnsemblBacteria; CAS10699; CAS10699; E2348C_3151.
DR   KEGG; ecg:E2348C_3151; -.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01175; tRNA_modifying_YgfZ; 1.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR023758; tRNA-modifying_YgfZ.
DR   InterPro; IPR045179; YgfZ/GcvT.
DR   InterPro; IPR017703; YgfZ/GcvT_CS.
DR   PANTHER; PTHR22602; PTHR22602; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR03317; ygfZ_signature; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Folate-binding; tRNA processing.
FT   CHAIN           1..326
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_1000164409"
FT   BINDING         27
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         189
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   326 AA;  36240 MW;  B8F539F57AB2460E CRC64;
     MAFTPFPPRQ PTASARLPLT LMTLDDWALA TITGADSEKY MQGQVTADVS QMTEDQHLLA
     AHCDAKGKMW SNLRLFRDGD GFAWIERRSV REPQLTELKK YAVFSKVTIA PDDERVLLGV
     AGFQARAALA NLFSELPSRE KQVVKEGATT LLWFEHPAER FLIVIDEATA NMLTDKLRGE
     AELNNSQQWL ALNIEAGFPV IDAANSGQFI PQATNLQALG GISFKKGCYT GQEMVARAKF
     RGANKRALWL LKGSASRLPE AGEDLELKMG ENWRRTGTVL AAVKLEDGQV VVQVVMNNDM
     EPDSIFRVRD DANTLRIEPL PYSLEE