YJFC_ECOLI
ID YJFC_ECOLI Reviewed; 387 AA.
AC P33222; Q2M6B9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative acid--amine ligase YjfC;
DE EC=6.3.1.-;
GN Name=yjfC; OrderedLocusNames=b4186, JW4144;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-387.
RC STRAIN=K12;
RX PubMed=7961409; DOI=10.1128/jb.176.21.6583-6589.1994;
RA Landini P., Hajec L.I., Volkert M.R.;
RT "Structure and transcriptional regulation of the Escherichia coli adaptive
RT response gene aidB.";
RL J. Bacteriol. 176:6583-6589(1994).
RN [5]
RP LACK OF GLUTATHIONYLSPERMIDINE SYNTHETASE ACTIVITY, FUNCTION, ATP-BINDING,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=23097746;
RA Sui L., Warren J.C., Russell J.P., Stourman N.V.;
RT "Comparison of the functions of glutathionylspermidine synthetase/amidase
RT from E. coli and its predicted homologues YgiC and YjfC.";
RL Int. J. Biochem. Mol. Biol. 3:302-312(2012).
CC -!- FUNCTION: May be a ligase forming an amide bond. Shows ATPase activity.
CC Despite its similarity to the C-terminal synthetase domain of Gss, is
CC not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp,
CC glutathione (GSH), or GSH intermediates, from GSH and spermidine,
CC cysteine and glutamate, gamma-glutamylcysteine and spermidine, and
CC gamma-glutamylcysteine and glycine. Does not bind to Gsp.
CC {ECO:0000269|PubMed:23097746}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene does not affect the ability
CC to synthesize glutathionylspermidine. There is no visible differences
CC between wild-type and mutant strain growth in LB media.
CC {ECO:0000269|PubMed:23097746}.
CC -!- SIMILARITY: Belongs to the glutathionylspermidine synthase preATP-grasp
CC family. {ECO:0000305}.
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DR EMBL; U14003; AAA97082.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77143.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78187.1; -; Genomic_DNA.
DR EMBL; L20915; AAC18888.1; -; Genomic_DNA.
DR PIR; S56411; S56411.
DR RefSeq; NP_418607.1; NC_000913.3.
DR RefSeq; WP_000943959.1; NZ_LN832404.1.
DR AlphaFoldDB; P33222; -.
DR SMR; P33222; -.
DR BioGRID; 4263212; 5.
DR IntAct; P33222; 1.
DR STRING; 511145.b4186; -.
DR PaxDb; P33222; -.
DR PRIDE; P33222; -.
DR EnsemblBacteria; AAC77143; AAC77143; b4186.
DR EnsemblBacteria; BAE78187; BAE78187; BAE78187.
DR GeneID; 948699; -.
DR KEGG; ecj:JW4144; -.
DR KEGG; eco:b4186; -.
DR PATRIC; fig|1411691.4.peg.2515; -.
DR EchoBASE; EB1760; -.
DR eggNOG; COG0754; Bacteria.
DR HOGENOM; CLU_059175_0_0_6; -.
DR InParanoid; P33222; -.
DR OMA; DEIYWDE; -.
DR PhylomeDB; P33222; -.
DR BioCyc; EcoCyc:EG11812-MON; -.
DR PRO; PR:P33222; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF03738; GSP_synth; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..387
FT /note="Putative acid--amine ligase YjfC"
FT /id="PRO_0000169746"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 372..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 101
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 45020 MW; 41DB418793D81ABB CRC64;
MLRHNVPVRR DLDQIAADNG FDFHIIDNEI YWDESRAYRF TLRQIEEQIE KPTAELHQMC
LEVVDRAVKD EEILTQLAIP PLYWDVIAES WRARDPSLYG RMDFAWCGNA PVKLLEYNAD
TPTSLYESAY FQWLWLEDAR RSGIIPRDAD QYNAIQERLI SRFSELYSRE PFYFCCCQDT
DEDRSTVLYL QDCAQQAGQE SRFIYIEDLG LGVGGVLTDL DDNVIQRAFK LYPLEWMMRD
DNGPLLRKRR EQWVEPLWKS ILSNKGLMPL LWRFFPGHPN LLASWFDGEK PQIAAGESYV
RKPIYSREGG NVTIFDGKNN VVDHADGDYA DEPMIYQAFQ PLPRFGDSYT LIGSWIVDDE
ACGMGIREDN TLITKDTSRF VPHYIAG
