ID   YGFZ_VIBCH              Reviewed;         323 AA.
AC   Q9KPA1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=VC_2472;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95614.1; -; Genomic_DNA.
DR   PIR; B82071; B82071.
DR   RefSeq; NP_232101.1; NC_002505.1.
DR   RefSeq; WP_000384066.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KPA1; -.
DR   SMR; Q9KPA1; -.
DR   STRING; 243277.VC_2472; -.
DR   PRIDE; Q9KPA1; -.
DR   DNASU; 2613014; -.
DR   EnsemblBacteria; AAF95614; AAF95614; VC_2472.
DR   GeneID; 57741076; -.
DR   KEGG; vch:VC_2472; -.
DR   PATRIC; fig|243277.26.peg.2356; -.
DR   eggNOG; COG0354; Bacteria.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   BioCyc; VCHO:VC2472-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
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; Reference proteome; tRNA processing.
FT   CHAIN           1..323
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262903"
FT   BINDING         29
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         182
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   323 AA;  36038 MW;  5775B130787B089B CRC64;
     MDWQNRFSVL NLSSHDPLPE LMLTHLTGWG AITLVGADKK AYLQGQVTCN VVSLQEQQVT
     FGAHCDAKGK VWSVFRLFHH HDGYAMFQPQ SAMEVELREL KKYAIFSKVT IAESSDIALG
     VMGSQADAWI DTVSETTGDV RRIAGGTAVR MSPQRWLLLV NAEQAEQYVN AWQGLHVEQS
     LWTRMDIEEA VPVVTQTAQN EHIPQALNVQ AVDGISFTKG CYTGQETVAR AKYRGINKRA
     MYIVKGNLSA PLSQDEPVVL ERAVGENWRS AGALLTHYRF TDSIAIGLIV LPNDLEHDVK
     LRLAAQPDTR WHIQPLPYSL SDE