ID   MURF_BUCAI              Reviewed;         455 AA.
AC   P57315;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_02019};
DE            EC=6.3.2.10 {ECO:0000255|HAMAP-Rule:MF_02019};
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_02019};
DE   AltName: Full=UDP-MurNAc-pentapeptide synthetase;
GN   Name=murF {ECO:0000255|HAMAP-Rule:MF_02019}; OrderedLocusNames=BU220;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_02019};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02019}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02019}.
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DR   EMBL; BA000003; BAB12936.1; -; Genomic_DNA.
DR   RefSeq; NP_240050.1; NC_002528.1.
DR   RefSeq; WP_010896011.1; NC_002528.1.
DR   AlphaFoldDB; P57315; -.
DR   SMR; P57315; -.
DR   STRING; 563178.BUAP5A_216; -.
DR   EnsemblBacteria; BAB12936; BAB12936; BAB12936.
DR   KEGG; buc:BU220; -.
DR   PATRIC; fig|107806.10.peg.233; -.
DR   eggNOG; COG0770; Bacteria.
DR   HOGENOM; CLU_031507_4_0_6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001806; 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; 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; 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; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..455
FT                   /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT                   ligase"
FT                   /id="PRO_0000101696"
FT   BINDING         107..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   455 AA;  50452 MW;  E292D8E9290E67B7 CRC64;
     MISLSLKKIA LITNGTLYGA DLLINEIVID TKKIIPGCLF IALIGRKFDA HIFIHDALKK
     KCAAFVTQKN IKPHVPYIIV ENTSIALGQI AGWVRKKTKA KILAITGSCG KTSVKEMTAS
     ILRKNGNTIS TIDNLNNNIG VPMTLLQLKQ EHKYGVIELG ASKPGEIAYT SNISQPDIIL
     INNIHCAHLQ GFKSLLGVSK AKSEIFSGLK PNSTVIINLD SHHFSQWKKD IKNSNILFFS
     IKKKKYSNFF CSNIKIHIHG TSFTMHTPCG KINISLPFLG YQNISNALAA SAFSFALKIP
     LKKIKIGLLD TPIVSKRLES IILEPNKILI DDTYNSNVSS MISAIKVLER MPGYKILVTG
     DMAELGENSM MYHQMIGNTA NSSAINKIFS IGDMSSEITK IFNNGKHFLN KKKLSEYLKN
     VFLKKKKITI LVKGSRSTKM EKVVEDLIKE SKKKC
//