ID   MURD2_SALTO             Reviewed;         448 AA.
AC   A4X981;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305};
DE            EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000269|PubMed:28294606};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305};
DE            Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000303|PubMed:28294606};
GN   Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000303|PubMed:28294606};
GN   OrderedLocusNames=Strop_3005 {ECO:0000312|EMBL:ABP55442.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=28294606; DOI=10.1021/jacs.7b01221;
RA   Feng R., Satoh Y., Ogasawara Y., Yoshimura T., Dairi T.;
RT   "A glycopeptidyl-glutamate epimerase for bacterial peptidoglycan
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 139:4243-4245(2017).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC       {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000269|PubMed:28294606}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC         glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC         EC=6.3.2.53; Evidence={ECO:0000255|HAMAP-Rule:MF_02208,
CC         ECO:0000269|PubMed:28294606};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305|PubMed:28294606}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02208, ECO:0000305}.
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DR   EMBL; CP000667; ABP55442.1; -; Genomic_DNA.
DR   RefSeq; WP_012014220.1; NC_009380.1.
DR   AlphaFoldDB; A4X981; -.
DR   SMR; A4X981; -.
DR   STRING; 369723.Strop_3005; -.
DR   EnsemblBacteria; ABP55442; ABP55442; Strop_3005.
DR   KEGG; stp:Strop_3005; -.
DR   PATRIC; fig|369723.5.peg.3092; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_4_1_11; -.
DR   OMA; CNFENYL; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   HAMAP; MF_02208; MurD2_subfam; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   InterPro; IPR043687; MurD2.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..448
FT                   /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT                   /id="PRO_0000446509"
FT   BINDING         118..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02208"
SQ   SEQUENCE   448 AA;  46954 MW;  62F1275C5CA30C5E CRC64;
     MRLSDLRGRK VAVWGTGREG RAAVVAIAAH GPADLVAVDD GGSTVSPPWD GFLATAAPLV
     TGDAGAQRLA AADVVVRSPG VPNTHPWLAE LWRRQVPVTQ GTALWMADHA ARTVGVTGSK
     GKSTTSSLIS HLLAAVDQPN VFGGNIGVPT LDLPAADLYV LELSSYQCSD LTDSPRVAVV
     TALFPEHLDA HGGEREYYRD KLNLLAHGPE TVVVNGADPR LAAELGDRPV VRAGTPDTTH
     VAGGPDGTPW FHLGDQPLFP RAVLPLVGRH NEGNLCVALA VLDVLGVDVL ARRDTLAVAV
     AGFQGLAHRL TEIVDPSGLT FVDDTLATSP YAAMHAIDAY DGRALTVIVG GADRGLDYTP
     LRDHLAEREI TVIGVPDSGA RIVAALDGLP KVRCDVTGDL VEAVRLARRV TPAGGVVLLS
     PAAPSYGQFR NFEHRSEVFA QAVRDTAG