ID   YGIC_ECO57              Reviewed;         386 AA.
AC   P0ADT7; P24196;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Putative acid--amine ligase YgiC;
DE            EC=6.3.1.-;
GN   Name=ygiC; OrderedLocusNames=Z4395, ECs3926;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: May be a ligase forming an amide bond. Shows ATPase activity
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutathionylspermidine synthase preATP-grasp
CC       family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58177.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37349.1; -; Genomic_DNA.
DR   PIR; E85964; E85964.
DR   PIR; F91119; F91119.
DR   RefSeq; NP_311953.1; NC_002695.1.
DR   RefSeq; WP_000442860.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0ADT7; -.
DR   SMR; P0ADT7; -.
DR   STRING; 155864.EDL933_4263; -.
DR   PRIDE; P0ADT7; -.
DR   EnsemblBacteria; AAG58177; AAG58177; Z4395.
DR   EnsemblBacteria; BAB37349; BAB37349; ECs_3926.
DR   GeneID; 66673064; -.
DR   GeneID; 916245; -.
DR   KEGG; ece:Z4395; -.
DR   KEGG; ecs:ECs_3926; -.
DR   PATRIC; fig|386585.9.peg.4094; -.
DR   eggNOG; COG0754; Bacteria.
DR   HOGENOM; CLU_059175_0_0_6; -.
DR   OMA; QWNSLHE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..386
FT                   /note="Putative acid--amine ligase YgiC"
FT                   /id="PRO_0000169402"
FT   BINDING         100..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
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         336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         371..373
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            100
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  45026 MW;  5DB19CE4F3FE4783 CRC64;
     MERVSITERP DWREKAHEYG FNFHTMYGEP YWCEDAYYKL TLAQVEKLEE VTAELHQMCL
     KVVEKVIASD ELMTKFRIPK HTWSFVRQSW LTHQPSLYSR LDLAWDGTGE PKLLENNADT
     PTSLYEAAFF QWIWLEDQLN AGNLPEGSDQ FNSLQEKLID RFVELREQYG FQLLHLTCCR
     DTVEDRGTIQ YLQDCATEAE IATEFLYIDD IGLGEKGQFT DLQDQVISNL FKLYPWEFML
     REMFSTKLED AGVRWLEPAW KSIISNKALL PLLWEMFPNH PNLLPAYFAE DDHPQMEKYV
     VKPIFSREGA NVSIIENGKT IEAAEGPYGE EGMIVQQFHP LPKFGDSYML IGSWLVNDQP
     AGIGIREDRA LITQDMSRFY PHIFVE