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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (D-alanyl-D-alanine-adding enzyme) (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)

 F4EVD2_SELS3            Unreviewed;       966 AA.
F4EVD2;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
23-MAY-2018, entry version 58.
SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase {ECO:0000313|EMBL:AEC00778.1};
EC=6.3.2.10 {ECO:0000313|EMBL:AEC00778.1};
EC=6.3.2.13 {ECO:0000313|EMBL:AEC00778.1};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
Synonyms=murF {ECO:0000256|HAMAP-Rule:MF_02019};
ORFNames=Selsp_1823 {ECO:0000313|EMBL:AEC00778.1};
Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
Bacteria; Firmicutes; Negativicutes; Selenomonadales;
Selenomonadaceae; Selenomonas.
NCBI_TaxID=546271 {ECO:0000313|EMBL:AEC00778.1, ECO:0000313|Proteomes:UP000011124};
[1] {ECO:0000313|EMBL:AEC00778.1, ECO:0000313|Proteomes:UP000011124}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35185 / DSM 20758 / VPI D19B-28
{ECO:0000313|Proteomes:UP000011124};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
"The complete genome of Selenomonas sputigena DSM 20758.";
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
-!- 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; CP002637; AEC00778.1; -; Genomic_DNA.
RefSeq; WP_013740969.1; NZ_GG698596.1.
EnsemblBacteria; AEC00778; AEC00778; Selsp_1823.
KEGG; ssg:Selsp_1823; -.
eggNOG; ENOG4107EEN; Bacteria.
eggNOG; COG0769; LUCA.
eggNOG; COG0770; LUCA.
KO; K15792; -.
UniPathway; UPA00219; -.
Proteomes; UP000011124; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UP000011124};
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:AEC00778.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
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:UP000011124}.
DOMAIN 26 94 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 110 315 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 335 419 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
DOMAIN 526 598 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 609 802 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 826 902 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 112 118 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
NP_BIND 611 617 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
REGION 154 155 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 410 413 Meso-diaminopimelate binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOTIF 410 413 Meso-diaminopimelate recognition motif.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 31 31 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 153 153 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 181 181 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 187 187 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 386 386 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 464 464 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 468 468 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
MOD_RES 221 221 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 966 AA; 103109 MW; A652F89D4169576A CRC64;
MKTLAELAAL VEGAEIKGDA AAKIADIVHD SREVTEGTLF VAIEGLHVDG HSFIAQAVEK
GACAILTERE IEIPEGAAAV LRVPNLAAAL EVIVPFFHDY PSRKMRIIGI TGTNGKTTTS
YMTRAILREA GYKVGLIGTI QILVEDEALP IHNTTPDVVV LERTLAYMAR RGMDFVVMEV
SSHALDQNRV AGIEFDTAVF TNLTQDHLDY HKTLENYKRA KARLFDLVSR KGAKEGKTAV
VNDDDAAGET MLAHAKCAHL TYAVKKEAAL RAENIRVHAR GLELTLAGAF GRMDLSLGVT
GIFNVYNVMS AVGAALAERI APEAIKRALE AFKSVPGRFE LVDAGQAFSI IVDYAHTPDG
LENILNTARE IAAGRILTVF GCGGDRDRTK RPIMGRIAAA LSDVVLVTSD NPRTEDPARI
LDEVEVGVLE KIGDKCHEKI ADRRTAIVRA VALAEKDDIV IIAGKGHENY QILKDKTIHF
DDKEVAREAV AAREKSYAMH FSLADIERAA KAEVVRTAAD IAFSDIVTDT RKIAAGSLFV
ALQGERFDGA DFAAQAVEKG AAGVLVAVDT PEAKLPKTGV VLKAKDTLLA YQQIAAAWRR
KFSIPVVAIT GSNGKTTTKD LTAAVLGACL LVQKTAANYN NEIGLPLTLL GLRAAHEAAV
VEIGMRGLGQ IAALAPLAAP TVAIVTNVGE VHMELLGSIE NIARAKAELV EAVEPGGTVI
LNADDARVLA MREKAKAGVR VVTFGLSRDA DVRAVAVGKA EGGMRFMLEW KNERGRLERH
ELFLPMPGRH NVSNALAAIA AARVLGLSLA DVRRGLAVPP AQKMRFAVEK CGAYTFVNDA
YNASPVSTRA SLKTLAEMFA GRKIAVLGDM LELGSASKSG HASVGEEAAH LGFAAVLSRG
EESRFIAEAA KAGGVPLVER MTSHEAAAAR LKEILQPGDA VLFKGSRGMK MDEIIPLLKK
ALEAGK


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