ID   A0A068NF09_9ACTO        Unreviewed;       464 AA.
AC   A0A068NF09;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   11-DEC-2019, entry version 29.
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=FB03_00900 {ECO:0000313|EMBL:AIE82066.1};
OS   Actinotignum schaalii.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinotignum.
OX   NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82066.1, ECO:0000313|Proteomes:UP000035032};
RN   [1] {ECO:0000313|EMBL:AIE82066.1, ECO:0000313|Proteomes:UP000035032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82066.1,
RC   ECO:0000313|Proteomes:UP000035032};
RX   PubMed=25189588;
RA   Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA   Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA   Christensen J.J., Prag J., Thomsen T.R.;
RT   "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL   Genome Announc. 2:e00880-14(2014).
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-L-lysine = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC         alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57822, ChEBI:CHEBI:70758,
CC         ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.10;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02019,
CC         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; CP008802; AIE82066.1; -; Genomic_DNA.
DR   RefSeq; WP_026428580.1; NZ_CP008802.1.
DR   EnsemblBacteria; AIE82066; AIE82066; FB03_00900.
DR   KEGG; asg:FB03_00900; -.
DR   KO; K01929; -.
DR   OrthoDB; 1861122at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000035032; 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: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 {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:AIE82066.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136}.
FT   DOMAIN          29..101
FT                   /note="Mur_ligase"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          118..306
FT                   /note="Mur_ligase_M"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          327..405
FT                   /note="Mur_ligase_C"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   NP_BIND         120..126
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   464 AA;  46888 MW;  8E2C3B3E37C3E1B8 CRC64;
     MISMSSAEVI AAVGGTALAP LCDTEVTAAV IDTRAITPGA LFAAVKGARV DANTLSGQAR
     AAGASLILTE DGQAARAGGA EAERIIVVDD IPAALGRLAR HNLELARQVN PDLRVIAVTG
     SVGKTTTKDL LAAICRERGD VVAPPGSLNN EIGLPLTVLR VGASTATLVA EMGADHIGNL
     AYLTSIAPPD IAVVLVVARA HLGEFGGIEN VARAKAELVE GLREDGIAIL NADDPRVAAM
     AGQVASGRVR TFGRVHPADV TATDITLGSD GRASFTLHMN DGAAAVNLGL VGEHQVMNAL
     AAATAAAAAG VSLPAIVAGL SSGPASAHRM DVFRRGSTLI IDDSYNANPD SMRAGIAALG
     QLGSGRKAAI LGDMLELGDA SREEHLALLP ALEAAGVSLL IAVGPQMAAL AEAARDAGIT
     ARAVGAWEEA EAELSDMLNE DGALLIKGSH GSGVWHIATR LKGE
//