ID   GCS2_ECOLU              Reviewed;         372 AA.
AC   B7N9I5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=ECUMN_0671;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / 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; CU928163; CAR11886.1; -; Genomic_DNA.
DR   RefSeq; WP_001130641.1; NC_011751.1.
DR   RefSeq; YP_002411432.1; NC_011751.1.
DR   AlphaFoldDB; B7N9I5; -.
DR   SMR; B7N9I5; -.
DR   STRING; 585056.ECUMN_0671; -.
DR   EnsemblBacteria; CAR11886; CAR11886; ECUMN_0671.
DR   KEGG; eum:ECUMN_0671; -.
DR   PATRIC; fig|585056.7.peg.868; -.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000007097; 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_1000148217"
SQ   SEQUENCE   372 AA;  41692 MW;  8485D53EE0EB94EF 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 KHQEKDYLLY KFNRFQACRY GLEGVITDPH
     TGDRRSLTED TLRLLEKIAP SAHKIGASSA IEALHRQVVS GLNEAQLMRD FVADGGSLIG
     LVKKHCEIWT GE