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Multifunctional fusion protein [Includes: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase); UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (EC 6.3.2.10) (D-alanyl-D-alanine-adding enzyme)]

 M1LYZ3_9PROT            Unreviewed;       979 AA.
M1LYZ3;
01-MAY-2013, integrated into UniProtKB/TrEMBL.
01-MAY-2013, sequence version 1.
18-JUL-2018, entry version 46.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|HAMAP-Rule:MF_02019};
Includes:
RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
Includes:
RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019};
EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019};
AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
Synonyms=murE {ECO:0000256|HAMAP-Rule:MF_00208};
ORFNames=ST1E_0984 {ECO:0000313|EMBL:AGF49276.1};
Candidatus Kinetoplastibacterium galatii TCC219.
Bacteria; Proteobacteria; Betaproteobacteria;
Candidatus Kinetoplastibacterium.
NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF49276.1, ECO:0000313|Proteomes:UP000011658};
[1] {ECO:0000313|EMBL:AGF49276.1, ECO:0000313|Proteomes:UP000011658}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TCC219 {ECO:0000313|EMBL:AGF49276.1};
PubMed=23345457;
Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J.,
Matveyev A.V., Teixeira M.M., Camargo E.P., Buck G.A.;
"Genome evolution and phylogenomic analysis of candidatus
kinetoplastibacterium, the betaproteobacterial endosymbionts of
strigomonas and angomonas.";
Genome Biol. Evol. 5:338-350(2013).
-!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to
the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
(UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- FUNCTION: Involved in cell wall formation. Catalyzes the final
step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
precursor of murein. {ECO:0000256|HAMAP-Rule:MF_02019,
ECO:0000256|RuleBase:RU004136}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate +
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-
diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-
glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-
acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
alanine. {ECO:0000256|HAMAP-Rule:MF_02019,
ECO:0000256|RuleBase:RU004136}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135,
ECO:0000256|SAAS:SAAS00951514}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}.
-!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
consequently, for the gamma-phosphate positioning of ATP.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
{ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
{ECO:0000256|HAMAP-Rule:MF_02019}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
-----------------------------------------------------------------------
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EMBL; CP003806; AGF49276.1; -; Genomic_DNA.
EnsemblBacteria; AGF49276; AGF49276; ST1E_0984.
KEGG; kga:ST1E_0984; -.
PATRIC; fig|1208921.3.peg.568; -.
KO; K15792; -.
OrthoDB; POG091H0082; -.
UniPathway; UPA00219; -.
Proteomes; UP000011658; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.40.1190.10; -; 2.
Gene3D; 3.90.190.20; -; 2.
HAMAP; MF_00208; MurE; 1.
HAMAP; MF_02019; MurF; 1.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
InterPro; IPR005863; UDP-N-AcMur_synth.
Pfam; PF01225; Mur_ligase; 2.
Pfam; PF02875; Mur_ligase_C; 2.
Pfam; PF08245; Mur_ligase_M; 2.
SUPFAM; SSF53244; SSF53244; 2.
SUPFAM; SSF53623; SSF53623; 2.
SUPFAM; SSF63418; SSF63418; 2.
TIGRFAMs; TIGR01085; murE; 1.
TIGRFAMs; TIGR01143; murF; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951530};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523};
Complete proteome {ECO:0000313|Proteomes:UP000011658};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951519};
Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:AGF49276.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
Membrane {ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951530};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548};
Reference proteome {ECO:0000313|Proteomes:UP000011658};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 957 978 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 33 105 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 117 320 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 358 434 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
DOMAIN 507 575 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 589 778 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 800 878 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 119 125 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
NP_BIND 591 597 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
REGION 162 163 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 424 427 Meso-diaminopimelate binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOTIF 424 427 Meso-diaminopimelate recognition motif.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 35 35 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 189 189 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 197 197 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 400 400 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 476 476 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 480 480 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
MOD_RES 229 229 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 979 AA; 108089 MW; D2E564BE1B627815 CRC64;
MSEFSYRSDH VYDISFLISW LKKRTYENSR LCSDSRCVSP GDVFIACSGY QTSGYFYIDD
AVSNGASAVL IDFVNNLESL VIDKDNVLVV SNLSKMLGDL ANQWYGNSSN KITLIAVTGT
NGKTSCVQWI AQALNNYGFL CGTIGTLGAF IPGNKLLYKG LTTPDVLSLH WIIFMMYRLG
VKIVAMEASS IGLEEGRLCG LNIKVAAFTN LTSDHLDYHK DIYSYERSKS HLFSILGIEK
FIINLDDSFG KRLSKKLPRS KSLLFSTEDI NPFADVYATD IRSNISGQVF LLKFHDNSLH
INIDVIGNYN ISNILLVVSV LIALNLPIDV IPKMIESLTS IPGRLQRVIP IKIGKLAFPT
VLVDFAHTKD ALFNVLKTLN PIAKNSGGKL ISLFGCGGNR DISKRPEMTK VAISYSDMVF
ITSDNPRMEN PDSIIEDMLS GVFSDTSSVH VEPNRALSIL LSIYSAKDKD IVLLAGKGHE
SYQENSNKKI FFDDCQWARL AMLLPVIKGI SIDTRSLKSD ELFIAIVGDK FDAHDYLNKA
KDAGSCAAVV SRRVEGVNIP QILVDDTKDA LMCIGSTYRR KYNLPVVAVV GSNGKTTTKE
MIAKILVDIY EKKNCLITDG NLNNSIGVPL TLSRLRGNHK AAVLELGMNH AGEIGILSSI
SAPTIVVITN AQREHQEFLG NVYNVAVENG SSIKFLPSNG IVVYPGDDKY SGLWDSITGK
LDSVTFGFSD DCDVYAKDIK CGCNNVSCNL VFKNREHPFI LPIPGEHNLR NALASISVSI
AMDLKLTDSM KSLESFESIC GRMKFYQLNE NILLIDDTYN SNPDSALAAI DVLKIQPGVK
ILVFGDMGET GSGFVELHKE IGFYAINNGI DKLITIGMNS KHTAFAFGIN AIVCESIEDI
VSLLTKYEKA SILIKGSRFM AMEDIVRSFS KKYVIGTRSV FKISIFFNIQ FYLFHNLIVR
AFFAFITSSI ISFLIFLLL


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