ID   GCS2_ECO57              Reviewed;         372 AA.
AC   Q8XBX1; Q7AGS4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   Name=ybdK; OrderedLocusNames=Z0720, ECs0619;
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: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01609};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
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DR   EMBL; AE005174; AAG54914.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34042.1; -; Genomic_DNA.
DR   PIR; C90706; C90706.
DR   PIR; F85556; F85556.
DR   RefSeq; NP_308646.1; NC_002695.1.
DR   RefSeq; WP_001130633.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XBX1; -.
DR   SMR; Q8XBX1; -.
DR   STRING; 155864.EDL933_0645; -.
DR   EnsemblBacteria; AAG54914; AAG54914; Z0720.
DR   EnsemblBacteria; BAB34042; BAB34042; ECs_0619.
DR   GeneID; 916978; -.
DR   KEGG; ece:Z0720; -.
DR   KEGG; ecs:ECs_0619; -.
DR   PATRIC; fig|386585.9.peg.727; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..372
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218197"
SQ   SEQUENCE   372 AA;  41684 MW;  0F140C9D9B08F974 CRC64;
     MPLPDFHVSE PFTLGIELEM QVVNPPGYDL SQDSSMLIDA VKNKITAGEV KHDITESMLE
     LATDVCRDIN QAAGQFSAMQ KVVLQAAADH HLEICGGGTH PFQKWQRQEV CDNERYQRTL
     ENFGYLIQQA TVFGQHVHVG CASGDDAIYL LHGLSRFVPH FIALSAASPY MQGTDTRFAS
     SRPNIFSAFP DNGPMPWVSN WQQFEALFRC LSYTTMIDSI KDLHWDIRPS PHFGTVEVRV
     MDTPLTLSHA VNMAGLIQAT AHWLLTERPF KHKEKDYLLY KFNRFQACRY GLEGVITDPY
     TGDRRPLTED TLRLLEKIAP SAHKIGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG
     LVKKHCEIWA GD