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Database: UniProt
Entry: A0A0J5L3L3_PLUGE
LinkDB: A0A0J5L3L3_PLUGE
Original site: A0A0J5L3L3_PLUGE 
ID   A0A0J5L3L3_PLUGE        Unreviewed;       438 AA.
AC   A0A0J5L3L3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000256|HAMAP-Rule:MF_00639,
GN   ECO:0000313|EMBL:KMK13395.1};
GN   ORFNames=ABW06_12185 {ECO:0000313|EMBL:KMK13395.1};
OS   Pluralibacter gergoviae (Enterobacter gergoviae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK13395.1, ECO:0000313|Proteomes:UP000036196};
RN   [1] {ECO:0000313|EMBL:KMK13395.1, ECO:0000313|Proteomes:UP000036196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS81F13 {ECO:0000313|EMBL:KMK13395.1,
RC   ECO:0000313|Proteomes:UP000036196};
RA   Greninger A.L., Miller S.;
RT   "Genome sequences of Pluralibacter gergoviae.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC         glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00639,
CC         ECO:0000256|RuleBase:RU003664};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMK13395.1}.
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DR   EMBL; LDZF01000011; KMK13395.1; -; Genomic_DNA.
DR   RefSeq; WP_048279047.1; NZ_VWRP01000011.1.
DR   AlphaFoldDB; A0A0J5L3L3; -.
DR   STRING; 61647.LG71_24645; -.
DR   PATRIC; fig|61647.15.peg.569; -.
DR   eggNOG; COG0771; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000036196; Unassembled WGS sequence.
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:UniProtKB-UniRule.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   NCBIfam; TIGR01087; murD; 1.
DR   PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   Pfam; PF21799; MurD-like_N; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00639};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00639};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036196}.
FT   DOMAIN          110..280
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          301..366
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         112..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   438 AA;  46742 MW;  ED9C8AEA4D62AE7F CRC64;
     MADYQGKNVV IIGLGLTGLS CVDFFIDRGV TPRVMDTRSA PPGLDKLPEG VERYLGGLND
     DWLLAADLIV ASPGIALAHP SLSAAADAGV EIVGDIELFC REAQAPVIAI TGSNGKSTVT
     TLVGEMAKAA GVNVGVGGNI GLPALMLLDV SRELYVLELS SFQLETTSSL RAVAATILNV
     TEDHMDRYPF GLQQYRAAKL RVYENAKTCV VNADDALTMP VRGADDRCVS FGVNIGDYHL
     NRQQGETWLR VKGEKVLNVK EMKLSGQHNY SNALAALALA DAAGLPRASS LKALTTFTGL
     AHRFQLALEH NGVRWINDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS ADFTPLTALI
     GGDNIRLWCF GRDGDELAAL RPDAATRTET MEEAMRLIAP QLRPGDMVLL SPACASLDQF
     KNFEQRGDIF TRLAKELG
//
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