ID V5XE53_MYCNE Unreviewed; 473 AA.
AC V5XE53;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE EC=6.3.2.8 {ECO:0000256|ARBA:ARBA00012211, ECO:0000256|HAMAP-Rule:MF_00046};
DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000256|HAMAP-Rule:MF_00046};
GN Name=murC {ECO:0000256|HAMAP-Rule:MF_00046};
GN ORFNames=D174_17775 {ECO:0000313|EMBL:AHC26297.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC26297.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC26297.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC26297.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
CC -!- FUNCTION: Cell wall formation. {ECO:0000256|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:0000256|ARBA:ARBA00001677, ECO:0000256|HAMAP-
CC Rule:MF_00046};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00046}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC Rule:MF_00046}.
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DR EMBL; CP006936; AHC26297.1; -; Genomic_DNA.
DR AlphaFoldDB; V5XE53; -.
DR KEGG; mne:D174_17775; -.
DR eggNOG; COG0773; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000018763; 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; 3.90.190.20; 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_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 NCBIfam; TIGR01082; murC; 1.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00046};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00046};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00046};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00046};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00046}; Reference proteome {ECO:0000313|Proteomes:UP000018763}.
FT DOMAIN 8..109
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 115..299
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 319..407
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 117..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00046"
SQ SEQUENCE 473 AA; 49283 MW; AA7B9F85CCB39A7D CRC64;
MPPELARVHM VGIGGAGMSG IARILLDRGG QVSGSDAKES RGIAALRARG AQIQIGHDAA
ALDMLDGGPT AVVTTHAAIP KTNPELVAAR QRGIPVILRP VVLAKLMAGD RTLMVTGTAG
KTTTTSMLIV ALQHSGFDPS FAVGGDLGAA GTNAHHGSGP YFVAEADESD GSLVQYRPDI
AVVTNIEADH LDFFGTEQAY VDVFDAFIER LQPGGALVVC VDDPGAAALA ERTEALGIRV
LRYGSSGADL AGALLDWEQR GTRAVATVQL AGEPAPRTMR LAVPGRHMAL NALAALLAAV
EAGAPPDAVL EALADFEGVR RRFELVGVRS GVRVFDDYAH HPTKVTAALT AVRTLAAESQ
GRAIVVFQPH LYSRTQTFAK EFGAALSLAD EAFVLDVYAA REQPIAGISG RSIVDHVTVP
VHYVPDFSAV ARRVAEITRP GDVVVTMGAG DVTLLGNEIL DAVGGRADRA ADR
//
