ID   YGFZ_YERPS              Reviewed;         330 AA.
AC   Q666S2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=YPTB3174;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH22412.1; -; Genomic_DNA.
DR   RefSeq; WP_011192958.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q666S2; -.
DR   SMR; Q666S2; -.
DR   EnsemblBacteria; CAH22412; CAH22412; YPTB3174.
DR   GeneID; 66844395; -.
DR   KEGG; ypo:BZ17_3437; -.
DR   KEGG; yps:YPTB3174; -.
DR   PATRIC; fig|273123.14.peg.3608; -.
DR   OMA; VNFKKGC; -.
DR   Proteomes; UP000001011; 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..330
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262911"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         190
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   330 AA;  35908 MW;  4563975A25FCB57F CRC64;
     MAYHTPFAAQ PPVASSGLPL TLISLDDWAL VTLTGADRVK YLQGQVTADI DALSADQHVL
     CAHCDAKGKM WSNLRLFYRG EGLAFIERRS LLDNQLSELK KYAVFSKVVI APQPDAVLIG
     VAGSQAKTAL AEIFTELPSA EHPVTQMGNS TLLHFSLPAE RFLLVTDTEQ AQQLVEKLAG
     RAQFNDSKQW LALDIEAGFP IIDAANSAQF IPQATNIQAL NGISFTKGCY TGQEMVARAK
     YRGANKRALY WLAGNASRVP AAGEDLEWQL GENWRRTGTV LSAIQLNDGT VWVQAVLNND
     LAADSVLRVR DDALGTLAIQ PLPYSLAEDK