ID   YGFZ_SALPC              Reviewed;         326 AA.
AC   C0PY21;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   Name=ygfZ {ECO:0000255|HAMAP-Rule:MF_01175}; OrderedLocusNames=SPC_3108;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(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; CP000857; ACN47195.1; -; Genomic_DNA.
DR   RefSeq; WP_000874173.1; NC_012125.1.
DR   AlphaFoldDB; C0PY21; -.
DR   SMR; C0PY21; -.
DR   EnsemblBacteria; ACN47195; ACN47195; SPC_3108.
DR   KEGG; sei:SPC_3108; -.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   Proteomes; UP000001599; 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; 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   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_1000164412"
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;  35914 MW;  CC000C6F47DD3CE3 CRC64;
     MAFISFPPRH PSSSARLPLT LIALDDWALS TITGVDSEKY IQGQVTADVS QMTEQQHLLA
     AHCDAKGKMW STLRLFRERD GFAWIERRSV LEAQLTELKK YAVFSKVVIA PDDERVLLGV
     AGFQARAALA NVFSVLPNSE NQVVRDGAST LLWFEHPAER FLLVTDVATA NMLTEKLHGE
     AELNNSQQWL ALDIEAGIPA IDAANSGQFI PQATNLQALG GISFKKGCYT GQEMVARAKF
     RGANKRALWL LAGKASRVPE AGEDLELQMG ENWRRTGAIL AATQLDDGQL LVQAVMNNDL
     EAESVFRVRD DANTLHIVPL PYSLEE