MURD_ACIB3
ID MURD_ACIB3 Reviewed; 448 AA.
AC B7H1N2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=ABBFA_003287;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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; CP001172; ACJ58865.1; -; Genomic_DNA.
DR RefSeq; WP_000908240.1; NZ_CP001172.1.
DR PDB; 7SIR; X-ray; 1.65 A; A=1-448.
DR PDBsum; 7SIR; -.
DR AlphaFoldDB; B7H1N2; -.
DR SMR; B7H1N2; -.
DR HOGENOM; CLU_032540_1_0_6; -.
DR OMA; CNFENYL; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006924; 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.
FT CHAIN 1..448
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_1000130819"
FT BINDING 112..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:7SIR"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:7SIR"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 365..371
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 401..411
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:7SIR"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:7SIR"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:7SIR"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:7SIR"
SQ SEQUENCE 448 AA; 47932 MW; 9C01945CDA3E63EC CRC64;
MLIQRGGLKV VAGLGISGVS AVNFLHEQGY QVAVTDSRPT PPGHDQIPAG VKTSFGQLDQ
ELLLQAEEII LSPGLAPQLP EIQAAIAKGI SVVGDIQLLR RATDVPIVAI TGSNAKSTVT
TLIGLMAKDA GKKVAVGGNL GRPALDLLKD QPELLVLELS SFQLETTSHL NAEVAVVLNM
SEDHLDRHGN MLGYHQAKHR IFQGAKKVVF NRDDALSRPL VPDTTPMQSF GLNAPDLNQY
GVLRDADGTL WLARGLQRLI KSSDLYIQGM HNVANALACL ALGEAIGLPM ESMLETLKQF
KGLEHRCEYV KTVHDVRYYN DSKGTNVGAT LAAIDGLGAA IEVKKGKVAL ILGGQGKGQD
FGPLRSSIEK YAKVVVLIGE DAPVIEQAIQ GATKILHAAT LKEAVELCQR ETQAEDVVLL
SPACASFDMF KSYNDRGQQF VACVNSLV
