ID   YGFZ_BAUCH              Reviewed;         325 AA.
AC   Q1LTU6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN   OrderedLocusNames=BCI_0149;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF13829.1; -; Genomic_DNA.
DR   RefSeq; WP_011520351.1; NC_007984.1.
DR   AlphaFoldDB; Q1LTU6; -.
DR   SMR; Q1LTU6; -.
DR   STRING; 374463.BCI_0149; -.
DR   EnsemblBacteria; ABF13829; ABF13829; BCI_0149.
DR   KEGG; bci:BCI_0149; -.
DR   HOGENOM; CLU_007884_6_1_6; -.
DR   OMA; VNFKKGC; -.
DR   OrthoDB; 1984573at2; -.
DR   Proteomes; UP000002427; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..325
FT                   /note="tRNA-modifying protein YgfZ"
FT                   /id="PRO_0000262884"
FT   BINDING         28
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
FT   BINDING         191
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01175"
SQ   SEQUENCE   325 AA;  37151 MW;  F90BB7A8CC561B06 CRC64;
     MHINFSYPYI IPSSHINLSL TLISLEEWAL ITFNGKDAVK YLQDQLACDV TSLKNNEYTF
     TVHCNTKGKV YSNVYFLHYQ DGFALITRKS VYANELNIFK KYAIFYTVNI NFHQNKILLG
     IAGLQVKDIL SNIFTTIPNR LCPVIHTMDT TILYLHQPAD RFLLITTNNI QNLILKKLTK
     YKIQTNNSKQ WLALDIAAGY PIIDQINSEL LLPQALNIEA LGGISFNKGC YLGQEAIART
     KYHNMNKKEL CFLSGKANRI PTASEKLEIK INNNWRYTGI VLAACKLKNN IWIQVVLNRN
     LAIDSILRVR GDITSVFHLC PLNYL