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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)

 A0A1V4GSA1_MORLA        Unreviewed;       501 AA.
A0A1V4GSA1;
07-JUN-2017, integrated into UniProtKB/TrEMBL.
07-JUN-2017, sequence version 1.
16-JAN-2019, entry version 10.
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};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
ORFNames=B5J94_09515 {ECO:0000313|EMBL:OPH35487.1};
Moraxella lacunata.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Moraxellaceae; Moraxella.
NCBI_TaxID=477 {ECO:0000313|EMBL:OPH35487.1, ECO:0000313|Proteomes:UP000191025};
[1] {ECO:0000313|Proteomes:UP000191025}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 4441 {ECO:0000313|Proteomes:UP000191025};
Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
Engstrand L., Kristiansson E., Moore E.;
"Draft genome sequence of Moraxella equi CCUG 4950T type strain.";
Submitted (MAR-2017) 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}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-
muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-
acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-
diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791,
ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
-!- 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}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135}.
-!- 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}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OPH35487.1}.
-----------------------------------------------------------------------
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EMBL; MXAN01000065; OPH35487.1; -; Genomic_DNA.
RefSeq; WP_062500220.1; NZ_MXAN01000065.1.
UniPathway; UPA00219; -.
Proteomes; UP000191025; Unassembled WGS sequence.
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: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; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00208; MurE; 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; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
TIGRFAMs; TIGR01085; murE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Complete proteome {ECO:0000313|Proteomes:UP000191025};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:OPH35487.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135}.
DOMAIN 119 324 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 346 429 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 121 127 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 163 164 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 419 422 Meso-diaminopimelate binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOTIF 419 422 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 190 190 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 196 196 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 198 198 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 395 395 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 472 472 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 476 476 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
MOD_RES 230 230 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 501 AA; 54255 MW; ADA2F4D247E9FB96 CRC64;
MTTFNDFAEI LQPHVSDMDW GCIKDLLIAG FVSDSRKVAG GEIFVLLSVN PDIKSKAKGY
IDSNNSQAVL SEISASDMGV DNTKMPIVHI ANLRLILGDL VKAYLQKTGA VDLPKVVAVT
GTNGKTTISQ LTAQLLSLAN HKTAVMGTAG NGILPNLSPS THTTLEVVAL QHAIYDYAKA
EVACIALEAS SHGLHQHRLQ GVPITVAVYS NLSRDHLDYH ADMDDYAGAK ARLFDKALFP
TLTHAVINAD DEFSEIFIRQ AKQSGLIIWT YSTKDSTADF FAKHISPSLN GVELVIQTPQ
GEMTVKSPLL GLFNVANLLA SIGASLAMNV SFDEIVNNIK HLKGARGRME QVPSERGSFI
VDYAHTPDAL TQVLTSLKAH CTGKLIAVFG CGGDRDKGKR PLMAQAGLAL ADRVILTADN
PRSENPNAIL SDMQVGMTCD DHYRTVIEPD RKRAIELAIK EAGEQDIVVI AGKGHETYQE
IQGVRYDFDD VAVVRELLNK K


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