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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)]

 A0A158M8B0_9BORD        Unreviewed;       940 AA.
A0A158M8B0;
08-JUN-2016, integrated into UniProtKB/TrEMBL.
08-JUN-2016, sequence version 1.
16-JAN-2019, entry version 24.
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=murE {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000313|EMBL:KAK98113.1};
Synonyms=murF {ECO:0000256|HAMAP-Rule:MF_02019};
ORFNames=L497_0014 {ECO:0000313|EMBL:KAK98113.1};
Bordetella holmesii CDC-H585-BH.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK98113.1, ECO:0000313|Proteomes:UP000026682};
[1] {ECO:0000313|EMBL:KAK98113.1, ECO:0000313|Proteomes:UP000026682}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK98113.1,
ECO:0000313|Proteomes:UP000026682};
Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C.,
Cassiday P., Tondella M.L., Liao P., Zimmerman J., Meert K.,
Wessel D., Berger J., Dean J.M., Holubkov R., Burr J., Liu T.,
Brinkac L.M., Sanka R., Kim M., Losada L.;
"Genome sequence of Bordetella holmseii.";
Submitted (MAR-2014) 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:
Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-
L-alanyl-gamma-D-glutamyl-L-lysine = ADP + H(+) + phosphate +
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-
D-alanyl-D-alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57822,
ChEBI:CHEBI:70758, ChEBI:CHEBI:83903, ChEBI:CHEBI:456216;
EC=6.3.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_02019,
ECO:0000256|RuleBase:RU004136};
-!- 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,
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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KAK98113.1}.
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EMBL; JFZZ01000019; KAK98113.1; -; Genomic_DNA.
RefSeq; WP_005018819.1; NZ_JFZZ01000019.1.
EnsemblBacteria; KAK98113; KAK98113; L497_0014.
GeneID; 23432386; -.
PATRIC; fig|1331206.3.peg.526; -.
UniPathway; UPA00219; -.
Proteomes; UP000026682; 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: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};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000026682};
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:KAK98113.1};
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}.
DOMAIN 29 101 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 113 314 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 335 430 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
DOMAIN 500 573 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 583 773 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 793 876 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 115 121 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
NP_BIND 585 591 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
REGION 158 159 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}.
COILED 662 682 {ECO:0000256|SAM:Coils}.
MOTIF 419 422 Meso-diaminopimelate recognition motif.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 30 30 UDP-MurNAc-L-Ala-D-Glu; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 32 32 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 185 185 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 191 191 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 193 193 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 395 395 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 470 470 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 474 474 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
MOD_RES 225 225 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 940 AA; 98074 MW; CE273A16466D7999 CRC64;
MSHVRTVAGS VQPVLQDLRG RVGAQADLHL DSREVRPGDV FLACRGVHGD GRLYIEQALA
AGAAAVVYDA DGLSLSLPRD TRLMAVAGLR AMLGALADAW YGEPSASLNV LAVTGTNGKT
SCVHWLAQAL TGLGKPCGTI GTLGGVLPDG RSLGGSLTTP DVVTVHRWLA AMRDAGAQAV
AMEASSIGLE QGRMDHVRLV VAGFTNLTRD HLDYHGTMQN YEAAKALLFN WPGLQAAVIN
ADDPAGQRLL ATLPAGLASG YSIESADAEI YVCDLQATAH GQVFTLRTAQ GEAQVVTSLL
GRHNVSNLLL VAGMLLKLGW PVSAVTRQIA AAAAVDGRLQ TVTALPLAAP LTSPLVVVDY
AHTPDALARA LSALRPVAQA RGGALVCLFG CGGDRDPGKR PEMGRIASGL ADRIIVSSDN
PRSESPQAII EQILAGVGQS GSVQTQVDRA LAILQTIWAS RPEDIVLLAG KGHETYQEIA
GRKVAFDDRE WARAAFALSH VSGVSTDTRS IAAGQLFVAL AGESFDGHDY LAQAAAAGAC
AAVVAHAVAD AALPQLVLGD TRQALGRLAK AWRSRFVLPA IAVTGSNGKT TTKEMISAVL
ADWQGQAHRL ATAGNFNNDI GLPLTLLRLR QEHRAAVFEL GMNHPGEIAL LAQMAQPSVA
LVNNAQREHQ EFMHTVEAVA RENGAVIAAL PDDGVAVYPG DDRYTAVWDE LAGARRVLRF
GLQPGLDVYA QDVRADLMGT LCRVVTPAGV AELALPVPGE HNLRNALAAI ACALAAGAPL
ASAIRALQGF AAVKGRMQRK EMSDGTLLID DTYNANPDSV RAAIEVLAQL PGPRALVLGD
MGEVGDNGPA MHREVGGYAR DHGIDALFTL GDASRAAAAE FGATALACAS VDEVVAALRG
LGAASVLVKG SRFMRMERVV TAFSVNDNQT ALGQEDKHAA


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