ID   GCS2_ECO7I              Reviewed;         372 AA.
AC   B7NLU0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=ECIAI39_0556;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928164; CAR16693.1; -; Genomic_DNA.
DR   RefSeq; WP_001130675.1; NC_011750.1.
DR   RefSeq; YP_002406582.1; NC_011750.1.
DR   AlphaFoldDB; B7NLU0; -.
DR   SMR; B7NLU0; -.
DR   STRING; 585057.ECIAI39_0556; -.
DR   EnsemblBacteria; CAR16693; CAR16693; ECIAI39_0556.
DR   KEGG; ect:ECIAI39_0556; -.
DR   PATRIC; fig|585057.6.peg.590; -.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000000749; 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.
FT   CHAIN           1..372
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_1000189576"
SQ   SEQUENCE   372 AA;  41734 MW;  E7ED0C16BEC0DE41 CRC64;
     MPLPDFHVSE PFTLGIELEM QVVNPPSYDL SQDSSMLIDA VKNKITVGEV KHDITESMLE
     LATDVCRDIN QAAGQFSAMQ KVVLQAAADH HLEICGGGTH PFQKWQRQEV CDNERYQRTL
     ENFGYLIQQA TVFGQHVHVG CASGDDAIYL LHGLSRFVPH FIALSAASPY MQGTDTRFAS
     SRPNIFSAFP DNGPMPWVSN WQQFEALFRC LSYTTMIDSI KDLHWDIRPS PHFGTVEVRV
     MDTPLTLSHA VNMAGLIQAT AHWLLTERPF KHQEKDYLLY KFNRFQACRY GLEGVITDPH
     TGDRRPLTED TLRLLEKIAP SAHKMGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG
     LVKKHCEIWA GD