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Database: UniProt
Entry: A0A3G8ZLF3_9ACTN
LinkDB: A0A3G8ZLF3_9ACTN
Original site: A0A3G8ZLF3_9ACTN 
ID   A0A3G8ZLF3_9ACTN        Unreviewed;       487 AA.
AC   A0A3G8ZLF3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ECO:0000313|EMBL:AZI57665.1};
GN   ORFNames=EH165_05365 {ECO:0000313|EMBL:AZI57665.1};
OS   Nakamurella antarctica.
OC   Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC   Nakamurella.
OX   NCBI_TaxID=1902245 {ECO:0000313|EMBL:AZI57665.1, ECO:0000313|Proteomes:UP000268084};
RN   [1] {ECO:0000313|EMBL:AZI57665.1, ECO:0000313|Proteomes:UP000268084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14-144 {ECO:0000313|EMBL:AZI57665.1,
RC   ECO:0000313|Proteomes:UP000268084};
RA   Da X.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AZI57665.1, ECO:0000313|Proteomes:UP000268084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14-144 {ECO:0000313|EMBL:AZI57665.1,
RC   ECO:0000313|Proteomes:UP000268084};
RA   Peng F.;
RT   "Nakamurella antarcticus sp. nov., isolated from Antarctica South Shetland
RT   Islands soil.";
RL   Submitted (DEC-2018) 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}.
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DR   EMBL; CP034170; AZI57665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8ZLF3; -.
DR   KEGG; nak:EH165_05365; -.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000268084; Chromosome.
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:AZI57665.1};
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:UP000268084}.
FT   DOMAIN          30..89
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          118..307
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          332..411
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         120..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   487 AA;  49944 MW;  9E6FC0945963A70E CRC64;
     MKSMTVSEVA EAIGTPILGS AKDATDDSGV TSVEFDTRKV SPGALFVALV GERVDGHDFV
     DAAVAAGAVA VLGSKDLDID VPLLRVADND AVLQALAELA ARSAAALTAQ GQLTTIGITG
     SAGKTSTKDL IAALASAAGS TIAPPESFNN ELGHPYTVLR ATEQTRFLVL ELSARGPGHV
     AMLAKVAPPR IGVVLNVGSA HIGEFGSVDG IAQAKSELVQ ALPAAADGGV AILNADDSRV
     AAMATRTRAR VVTFGTHPGA DVRAENVTED HHARAGFTLM TPRGAVPVQL AVSGVHQVSN
     ALAAAAVGLE IGVSLQDIAQ VLGASGPASK WRMEITDRAD GVTVINDAYN ANPEAMKAAL
     KALVTIGTGR RRWAVLGEMA ELGEISRAAH DEIGRLVVRL GIERLIAVGA GVRGLHLGAQ
     LEGSWDGESE HVPDWEDAVR ILGDELRPGD VVLVKASRAV GLERVAHALL HGNPPASGDA
     DENGISE
//
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