MURF_MYCBO
ID MURF_MYCBO Reviewed; 510 AA.
AC P0A5L5; A0A1R3Y0E7; O06220; X2BK26;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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};
GN OrderedLocusNames=BQ2027_MB2181C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00789.1; -; Genomic_DNA.
DR RefSeq; NP_855830.1; NC_002945.3.
DR RefSeq; WP_003411187.1; NC_002945.4.
DR AlphaFoldDB; P0A5L5; -.
DR SMR; P0A5L5; -.
DR EnsemblBacteria; SIU00789; SIU00789; BQ2027_MB2181C.
DR PATRIC; fig|233413.5.peg.2397; -.
DR OMA; VEMGANH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001419; 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; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 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 Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR SUPFAM; SSF63418; SSF63418; 1.
DR TIGRFAMs; TIGR01143; murF; 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.
FT CHAIN 1..510
FT /note="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
FT ligase"
FT /id="PRO_0000101702"
FT BINDING 136..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02019"
SQ SEQUENCE 510 AA; 51633 MW; 7BE83EDD1BAA2EC4 CRC64;
MIELTVAQIA EIVGGAVADI SPQDAAHRRV TGTVEFDSRA IGPGGLFLAL PGARADGHDH
AASAVAAGAA VVLAARPVGV PAIVVPPVAA PNVLAGVLEH DNDGSGAAVL AALAKLATAV
AAQLVAGGLT IIGITGSSGK TSTKDLMAAV LAPLGEVVAP PGSFNNELGH PWTVLRATRR
TDYLILEMAA RHHGNIAALA EIAPPSIGVV LNVGTAHLGE FGSREVIAQT KAELPQAVPH
SGAVVLNADD PAVAAMAKLT AARVVRVSRD NTGDVWAGPV SLDELARPRF TLHAHDAQAE
VRLGVCGDHQ VTNALCAAAV ALECGASVEQ VAAALTAAPP VSRHRMQVTT RGDGVTVIDD
AYNANPDSMR AGLQALAWIA HQPEATRRSW AVLGEMAELG EDAIAEHDRI GRLAVRLDVS
RLVVVGTGRS ISAMHHGAVL EGAWGSGEAT ADHGADRTAV NVADGDAALA LLRAELRPGD
VVLVKASNAA GLGAVADALV ADDTCGSVRP
