ID A0A0G9MSU1_9SPHN Unreviewed; 485 AA.
AC A0A0G9MSU1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
GN ORFNames=AAW00_12180 {ECO:0000313|EMBL:KLE33827.1};
OS Aurantiacibacter luteus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE33827.1, ECO:0000313|Proteomes:UP000053464};
RN [1] {ECO:0000313|EMBL:KLE33827.1, ECO:0000313|Proteomes:UP000053464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA37 {ECO:0000313|EMBL:KLE33827.1,
RC ECO:0000313|Proteomes:UP000053464};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter luteus KA37.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC murein. {ECO:0000256|HAMAP-Rule:MF_02019,
CC ECO:0000256|RuleBase:RU004136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC ChEBI:CHEBI:456216; EC=6.3.2.10; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC ECO:0000256|RuleBase:RU004136}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02019}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02019}.
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:KLE33827.1}.
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DR EMBL; LBHB01000003; KLE33827.1; -; Genomic_DNA.
DR RefSeq; WP_047004715.1; NZ_LBHB01000003.1.
DR AlphaFoldDB; A0A0G9MSU1; -.
DR STRING; 1581420.AAW00_12180; -.
DR PATRIC; fig|1581420.6.peg.2489; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053464; 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:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
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; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR HAMAP; MF_02019; MurF; 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; IPR035911; MurE/MurF_N.
DR InterPro; IPR005863; UDP-N-AcMur_synth.
DR NCBIfam; TIGR01143; murF; 1.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02019};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:KLE33827.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02019}; Reference proteome {ECO:0000313|Proteomes:UP000053464}.
FT DOMAIN 42..92
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 121..313
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 346..405
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 485 AA; 50576 MW; F7B3356A51306463 CRC64;
MSALAKTLRW PRKRDDAQRL ALWTSTEIAA ATGGTAYGEF QVSGVEMDSR DVVAGDLFVA
LKGEAMDGHR FVDTAFANGA AAALVDRPVD FPHVLVEDTT EALHALARAA RERATARVVG
VTGSVGKTGV KEAIFTALER SSRGAAHRSV RSYNNHVGVP LSLSRMPAKS RFGVFEMGMN
HAGEIAGLTA HVRPHVAVVT TIAPAHIENL GSEEAIADAK AEIFAGLQKG GTAVIPADSP
HFERLRDAAK AQGAKVVAFG RGAHADMRLL DAIPRVEGGA LVTAAMGDLR LCYTVAEPGE
HWIDNSLCVM AAVHAAGGDL GAAGLALAEM GGLKGRGARL RAKVPGGHAL VIDESYNANP
ASMRATLAQL GQTPATRRVA VLGSMKELGD FADRFHAQLA APVADAGVDY AVLVGPEMLA
LAREMGKLPR DTLGNRFSYA HCENAGEAIA ALQEFGLAGG DVVLVKGSNS VGLSRVVDHF
AAREG
//
