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UDP-N-acetylmuramyl-tripeptide synthetase (EC 6.3.2.-) (UDP-MurNAc-tripeptide synthetase)

 F7SFM4_LACJH            Unreviewed;       523 AA.
F7SFM4;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
22-NOV-2017, entry version 42.
RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
EC=6.3.2.- {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
ORFNames=PF01_01351 {ECO:0000313|EMBL:EGP13060.1};
Lactobacillus johnsonii pf01.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
Lactobacillus.
NCBI_TaxID=1037411 {ECO:0000313|EMBL:EGP13060.1, ECO:0000313|Proteomes:UP000003032};
[1] {ECO:0000313|EMBL:EGP13060.1, ECO:0000313|Proteomes:UP000003032}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=pf01 {ECO:0000313|Proteomes:UP000003032};
PubMed=21742886; DOI=10.1128/JB.05640-11;
Lee J.H., Chae J.P., Lee J.Y., Lim J.S., Kim G.B., Ham J.S., Chun J.,
Kang D.K.;
"Genome Sequence of Lactobacillus johnsonii PF01, Isolated from Piglet
Feces.";
J. Bacteriol. 193:5030-5031(2011).
-!- FUNCTION: Catalyzes the addition of an amino 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}.
-!- 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:EGP13060.1}.
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EMBL; AFQJ01000004; EGP13060.1; -; Genomic_DNA.
RefSeq; WP_004898025.1; NZ_AFQJ01000004.1.
ProteinModelPortal; F7SFM4; -.
EnsemblBacteria; EGP13060; EGP13060; PF01_01351.
PATRIC; fig|1037411.3.peg.1340; -.
UniPathway; UPA00219; -.
Proteomes; UP000003032; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; 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; 3.40.1390.10; -; 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; IPR035911; MurE/MurF_N.
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.
SUPFAM; SSF63418; SSF63418; 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:UP000003032};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:EGP13060.1};
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 118 338 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 359 444 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 119 125 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 165 166 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 41 41 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 192 192 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 200 200 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOD_RES 234 234 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 523 AA; 58009 MW; 509014936DFB5690 CRC64;
MSDSSISLNT CILILKEHHL LKSSAVQDAV PTKMDYISYD SRDIKTNTLF FCKGKGFRPT
YLSMAKDSGA TCYVAEQPYP EGKGMHALVV RDVTKAMALL SAAFYRFPQD DLYVVAFTGT
KGKTTSAYFL KGMLDQINGG RTALFSSVDD IVGPKPEDKF KASLTTPESL DLFRDMRTAV
DNGMTHLVME VSSQAYKKNR VFGLTYDLGF FLNITPDHIG PNEHPNFADY LHCKLQLMVN
SRKCIINAMS DHFDEIYAAA TTTTNPDSIY LFARNDFENP NLKQPIDFRF QSVETDMKET
EFKLFCASDK AKKLPIAGDY TLQMIGDFNE MNGTAAIIGA GLAGENYEEC AKGIRHVTIP
GRMEALPSKN HGTVIVDYAH NKASMMALMS FMQREFNNPK IIVVVGAPGD KGVSRRPGFS
ESLTAYADKA FLTTDDPGFE DPMDIAQEID AGIDHEKVDV TIELDREKAI HDAIAMSDKD
DIVLICGKGA DPYQKIRGVD TPYPTDIKVA ESVINELEKD DEE


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