YGFZ_CROS8
ID YGFZ_CROS8 Reviewed; 329 AA.
AC A7MR73;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000255|HAMAP-Rule:MF_01175};
GN OrderedLocusNames=ESA_00433;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU75730.1; -; Genomic_DNA.
DR RefSeq; WP_012123854.1; NC_009778.1.
DR AlphaFoldDB; A7MR73; -.
DR SMR; A7MR73; -.
DR EnsemblBacteria; ABU75730; ABU75730; ESA_00433.
DR KEGG; esa:ESA_00433; -.
DR PATRIC; fig|290339.8.peg.395; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OMA; VNFKKGC; -.
DR OrthoDB; 1984573at2; -.
DR Proteomes; UP000000260; 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..329
FT /note="tRNA-modifying protein YgfZ"
FT /id="PRO_1000065776"
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 329 AA; 36106 MW; D24E582E0EDEF1AA CRC64;
MAFTPFPPRQ PAASARLPLT LISLEDWALA TITGPDSEKY LQGQVTADVT ELGENQHLLV
AHCDAKGKMW SNLRLFRHGD GFAWIERRSV RDTQLAEMKK YAVFSKVTIA PNDDAVLLGV
AGFQARAALA NHFATLPDEQ NPRVVDGATT LLWFGLPAER FMVITDAETA SQLSDKLHGE
AQLNASAQWL ALDIEAGFPV IDAPNSNQFI PQATNIQALG GISFKKGCYA GQEMVARAKF
RGANKRSLWY LAGHGSRVPQ PGEDIEMQMG ENWRRTGTVL AAVQLDDGRL LAQVVMNNDL
ETGTLFRVRE ESGAHTLHIE PLPYSLEEA