YGFZ_ECOLU
ID YGFZ_ECOLU Reviewed; 326 AA.
AC B7N7E2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN Name=ygfZ {ECO:0000255|HAMAP-Rule:MF_01175}; OrderedLocusNames=ECUMN_3240;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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}.
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DR EMBL; CU928163; CAR14404.1; -; Genomic_DNA.
DR RefSeq; WP_000886049.1; NC_011751.1.
DR RefSeq; YP_002413923.1; NC_011751.1.
DR AlphaFoldDB; B7N7E2; -.
DR SMR; B7N7E2; -.
DR STRING; 585056.ECUMN_3240; -.
DR EnsemblBacteria; CAR14404; CAR14404; ECUMN_3240.
DR KEGG; eum:ECUMN_3240; -.
DR PATRIC; fig|585056.7.peg.3417; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR Proteomes; UP000007097; 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_1000138074"
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; 36136 MW; BBFB5A0352754736 CRC64;
MAFTPFPPRQ PTASARLPLT LITLDDWALA TITGADSEKY MQGQVTADVS QMTEDQHLLA
AHCDAKGKMW SNLRLFRDGD GFAWIERRSV REPQLTELKK YAVFSKVTIA PDDERVLLGV
AGFQARAALA NLFSELPSKE KQVVKEGATT LLWFEHPAER FLIVTDEATA NMLTDKLRGE
AELNNSQQWL ALNIEAGFPV IDAANSGQFI PQATNLQALG GISFKKGCYT GQEMVARAKF
RGANKRALWL LTGSASRLPE AGEDLELKMG ENWRRTGTVL AAVKLEDGQV VVQVVMNNDM
EPDSIFRVRD DANTLHIEPL PYSLEE
