YGFZ_ESCF3
ID YGFZ_ESCF3 Reviewed; 326 AA.
AC B7LPB2;
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=EFER_2834;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
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; CU928158; CAQ90328.1; -; Genomic_DNA.
DR RefSeq; WP_000886105.1; NC_011740.1.
DR AlphaFoldDB; B7LPB2; -.
DR SMR; B7LPB2; -.
DR EnsemblBacteria; CAQ90328; CAQ90328; EFER_2834.
DR KEGG; efe:EFER_2834; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR OrthoDB; 1984573at2; -.
DR BioCyc; EFER585054:EFER_RS14275-MON; -.
DR Proteomes; UP000000745; 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_1000138077"
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; 36216 MW; 7F75749AD2921FC0 CRC64;
MAFTPFPPRQ PTASARLPLT LMTLDDWALA TITGTDSEKY MQGQVTADVS QMTEDQHLLA
AHCDAKGKMW SNLRLFRDGD GFAWIERRSV RESQLTELKK YAVFSKVTIA PDDERVLLGV
AGFQARAALA NLFSELPSKE KQVIREGATT LLWFEHPAER FLIVTDEATA NTLTDKLRGE
AELNNSQQWL ALNIEAGFPV IDAANSGQFI PQATNLQALG GISFKKGCYT GQEMVARAKF
RGANKRALWL LAGSASRLPE AGEDLELKMG ENWRRTGTVL AAVKLEDGQV VVQVVMNNDM
EPDSIFRVRD DMNTLHIEPL PYSLEE