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Database: UniProt
Entry: A0A087BPY8_9BIFI
LinkDB: A0A087BPY8_9BIFI
Original site: A0A087BPY8_9BIFI 
ID   A0A087BPY8_9BIFI        Unreviewed;       546 AA.
AC   A0A087BPY8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019};
DE            EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019};
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=BMIN_0811 {ECO:0000313|EMBL:KFI73088.1};
OS   Bifidobacterium minimum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI73088.1, ECO:0000313|Proteomes:UP000029014};
RN   [1] {ECO:0000313|EMBL:KFI73088.1, ECO:0000313|Proteomes:UP000029014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI73088.1,
RC   ECO:0000313|Proteomes:UP000029014};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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   -!- 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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {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:KFI73088.1}.
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DR   EMBL; JGZD01000008; KFI73088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087BPY8; -.
DR   STRING; 1693.BMIN_0811; -.
DR   eggNOG; COG0770; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000029014; 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; 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   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; 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; 2.
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|HAMAP-Rule:MF_02019};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell wall biogenesis/degradation {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:KFI73088.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029014}.
FT   DOMAIN          28..97
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          114..322
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   REGION          378..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   546 AA;  55656 MW;  697CFF0D25D5F347 CRC64;
     MPISVARLCR VVGGSMVGDA TAPDSAVEQV VTDSRRVLPG TVFVAIKGER VDGHDFLDSA
     ARDGAVAAIV DHEVAGAGIA QIVVPDTVEA LGDVARASIA LRRDAEGDFT VIGITGSVGK
     TTTKDMLNAV LSTVGETVAP VGSFNNEIGL PLTALRVGPC TRFLIAEMGA NHGGEIAHLT
     SIVPPDISVV LKVGVAHLGE FGSVERIAQA KSEIVRGLVD GGTAVLNAGD SHVAAMAAIA
     PGDVLWFRDP DDPDCSAVCD DPAGSDDPGD GRSTLLSATD VRLDGHDRPS FTLDDGVVQA
     RVRLAIPGRH NVVNALAAAT VARHVGVGVD RIAAALSGVE HISPHRMAVS RVVRDGAEFT
     LIDDSFNANP DSMMAGLDGL ARWGDGPSSG PSSYESSSYE SSSSGPSSSE SPSCEPYRIA
     VLGAMLELGA DEDALHRSIG RYAVSCGADA VIAVGNGDGD GHLADLAGCL AQGAREAVGD
     DETAGRHGDV RVAVAEDSAQ ADIMVMRLVR GHPGSVVLLK GSHASGLSAL ASSWTVPGTG
     HDTGRP
//
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