ID A0A0G0FRS5_9BACT Unreviewed; 445 AA.
AC A0A0G0FRS5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate-2, 6-diaminopimelate ligase, UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase {ECO:0000313|EMBL:KKP90030.1};
DE EC=6.3.2.13 {ECO:0000313|EMBL:KKP90030.1};
GN Name=murE {ECO:0000313|EMBL:KKP90030.1};
GN ORFNames=UR95_C0004G0073 {ECO:0000313|EMBL:KKP90030.1};
OS Parcubacteria group bacterium GW2011_GWC1_36_108.
OC Bacteria.
OX NCBI_TaxID=1618894 {ECO:0000313|EMBL:KKP90030.1, ECO:0000313|Proteomes:UP000034191};
RN [1] {ECO:0000313|EMBL:KKP90030.1, ECO:0000313|Proteomes:UP000034191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|RuleBase:RU004135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000256|ARBA:ARBA00005898}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKP90030.1}.
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DR EMBL; LBRD01000004; KKP90030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0FRS5; -.
DR STRING; 1618894.UR95_C0004G0073; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000034191; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR NCBIfam; TIGR01085; murE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU004135};
KW Cell division {ECO:0000256|RuleBase:RU004135};
KW Cell shape {ECO:0000256|RuleBase:RU004135};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135};
KW Ligase {ECO:0000313|EMBL:KKP90030.1};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135}.
FT DOMAIN 40..265
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 286..373
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 445 AA; 49982 MW; 8D93EF21852E2E85 CRC64;
MHYIKKLFPQ NIKNLYHLAQ AVVANVWYGF PSRKLKVIGV TGTDGKTTTV QMVTKILEEA
GRKVAMASTI NFKINGVEEK NLSHFTTESA LTLQKFIKKA VDAGCEYLVL ETSSHSLDQY
RVWGVDYKTA VITNVTREHL DYHKTMEKYR EAKKKLFENV EKNKGTNIVN LDMENPNEFV
NFNVEKKYGY TTKIESTNLI NQNDNVKIKI VNAENIEIGI NGSSFEIGNF SAAKLAGMDE
KKSIRLNLQL PGLFNVENAL AATCVGLSEE IGIETIKDAL AKIKGVAGRM EAVENDLGLH
ILVDFALTPN ALERLYSTLF QAKKSDSKII AIFGSCGDRD RGKRPIMGGV VSKYADVVIL
TNDEPYYEKP EQIIEEIAVG IKNKTEGQNF WKIIDRREAI RKAIEIAQEG DIICITGMGD
FETMVVGDKK IPWNDRKVIE EELVR
//
