MURD_STRA5
ID MURD_STRA5 Reviewed; 451 AA.
AC Q8E186;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639};
DE EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639};
DE AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639};
GN Name=murD {ECO:0000255|HAMAP-Rule:MF_00639}; OrderedLocusNames=SAG0475;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000255|HAMAP-Rule:MF_00639}.
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:0000255|HAMAP-Rule:MF_00639};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC Rule:MF_00639}.
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DR EMBL; AE009948; AAM99377.1; -; Genomic_DNA.
DR RefSeq; NP_687505.1; NC_004116.1.
DR RefSeq; WP_000849681.1; NC_004116.1.
DR PDB; 3LK7; X-ray; 1.50 A; A=1-451.
DR PDBsum; 3LK7; -.
DR AlphaFoldDB; Q8E186; -.
DR SMR; Q8E186; -.
DR STRING; 208435.SAG0475; -.
DR DNASU; 1013278; -.
DR EnsemblBacteria; AAM99377; AAM99377; SAG0475.
DR KEGG; sag:SAG0475; -.
DR PATRIC; fig|208435.3.peg.473; -.
DR HOGENOM; CLU_032540_0_1_9; -.
DR OMA; CNFENYL; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q8E186; -.
DR Proteomes; UP000000821; 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: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; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 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 Pfam; PF02875; Mur_ligase_C; 1.
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 3D-structure; 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..451
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109094"
FT BINDING 119..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:3LK7"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:3LK7"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 277..293
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:3LK7"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:3LK7"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3LK7"
FT HELIX 434..449
FT /evidence="ECO:0007829|PDB:3LK7"
SQ SEQUENCE 451 AA; 48933 MW; 499B0ADCC9FA011E CRC64;
MKTITTFENK KVLVLGLARS GEAAARLLAK LGAIVTVNDG KPFDENPTAQ SLLEEGIKVV
CGSHPLELLD EDFCYMIKNP GIPYNNPMVK KALEKQIPVL TEVELAYLVS ESQLIGITGS
NGKTTTTTMI AEVLNAGGQR GLLAGNIGFP ASEVVQAAND KDTLVMELSS FQLMGVKEFR
PHIAVITNLM PTHLDYHGSF EDYVAAKWNI QNQMSSSDFL VLNFNQGISK ELAKTTKATI
VPFSTTEKVD GAYVQDKQLF YKGENIMSVD DIGVPGSHNV ENALATIAVA KLAGISNQVI
RETLSNFGGV KHRLQSLGKV HGISFYNDSK STNILATQKA LSGFDNTKVI LIAGGLDRGN
EFDELIPDIT GLKHMVVLGE SASRVKRAAQ KAGVTYSDAL DVRDAVHKAY EVAQQGDVIL
LSPANASWDM YKNFEVRGDE FIDTFESLRG E
