MURC_ACIB3
ID MURC_ACIB3 Reviewed; 482 AA.
AC B7GV74;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046};
DE EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046};
GN Name=murC {ECO:0000255|HAMAP-Rule:MF_00046};
GN OrderedLocusNames=ABBFA_000146;
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. {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine;
CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00046};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC Rule:MF_00046}.
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DR EMBL; CP001172; ACJ58378.1; -; Genomic_DNA.
DR RefSeq; WP_000075472.1; NZ_CP001172.1.
DR PDB; 6CAU; X-ray; 2.50 A; A=19-482.
DR PDBsum; 6CAU; -.
DR AlphaFoldDB; B7GV74; -.
DR SMR; B7GV74; -.
DR GeneID; 66395480; -.
DR HOGENOM; CLU_028104_2_2_6; -.
DR OMA; DITYQLR; -.
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:0008763; F:UDP-N-acetylmuramate-L-alanine 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_00046; MurC; 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; IPR000713; Mur_ligase_N.
DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_MurC.
DR Pfam; PF01225; Mur_ligase; 1.
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; TIGR01082; murC; 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..482
FT /note="UDP-N-acetylmuramate--L-alanine ligase"
FT /id="PRO_1000116611"
FT BINDING 129..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00046"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:6CAU"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6CAU"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 237..242
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:6CAU"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:6CAU"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:6CAU"
SQ SEQUENCE 482 AA; 52882 MW; 4F18E9DBFCAD79ED CRC64;
MSPTTAANQA KKLIKVPEMR RIKHIHFVGI GGAGMCGIAE VLANQGYKIS GSDIKASKTT
QQLEENGIKV YIGHEAENIK NANVLVVSTA IDPENPEVKA AIEQRIPIVR RAEMLGELMR
YRHGIAVAGT HGKTTTTSLL TTMLAEENLD PTYVIGGLLN STGVNAALGE SRFIVAEADE
SDASFLYLQP MAAIVTNIDA DHMDTYEGSF DKLKDTFVQF LHNLPFYGLA VVCGDDANIR
EILPRVGRPV ITYGFNEDND IRAIDVEQDG MRSHFTVLRK GREPLRLTIN QPGLHNVLNA
LAAIGVATDE GVSDEAISRA LKGFSGVGRR FQVQGEFELG EGNVKLVDDY GHHPKEVEAT
IKAARQSHPD RRLVMLFQPH RYSRTRDCFD DFIEVLSQVD QLLLLEVYPA GEKPIVGADS
RTLARSIRLR GQVEPILIDP VEGNLQNIMQ NVLQPNDLLL TQGAGNVGAI SVELAQHHLY
VK
