ID A0A0G0UIU0_9BACT Unreviewed; 632 AA.
AC A0A0G0UIU0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2, 6-diaminopimelate ligase {ECO:0000313|EMBL:KKR87451.1};
GN ORFNames=UU32_C0005G0010 {ECO:0000313|EMBL:KKR87451.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_41_10.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618577 {ECO:0000313|EMBL:KKR87451.1, ECO:0000313|Proteomes:UP000033858};
RN [1] {ECO:0000313|EMBL:KKR87451.1, ECO:0000313|Proteomes:UP000033858}
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 -!- 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:KKR87451.1}.
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DR EMBL; LCAE01000005; KKR87451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0UIU0; -.
DR PATRIC; fig|1618577.3.peg.105; -.
DR Proteomes; UP000033858; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd02540; GT2_GlmU_N_bac; 1.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000313|EMBL:KKR87451.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 1..46
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 67..181
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 231..310
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT DOMAIN 389..626
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 632 AA; 70437 MW; E3B4319488B06666 CRC64;
MITTDSRKVG PGDIFVAIKG RTVDGHNYID EAIKRGAVKI YSGRKKLAEL ASKFYGNPSK
KLKVIGVTGT KGKTTTCHMV AHILNKLGQK TGLISSITVP GYHVTTPETE DLHRMLKEMV
DEGCRYAVIE VSSHGIDQKR IAGVKFVAAV LTNIAPEHLD YHRTFENYKK IKMNFLKSAK
IKVMSPKSTK LKILPGEFNN LNAETALDVV VKLGFARKAA IDTFGSFTLP EGRLEEVKTD
KGFRVFIDFA HTPESLEAAL KYLKTITKGR LISVFGCAGE RDSRKRSKMG KISTQIADLS
VFTVEDSRIE NIFSILGRMK SKATLGKFMS IPERAEAITY ALSLAKRGDA IGIFGKGHEK
SMSYMGFEHL WSDREIIESL VKPKDGVSAI ILAAGKGTRM KSQKSKVLRE ICGRPMLSYT
LENLRRVGID DITIVVGFRK NLVVKRFGGA VKFAIQKTPK GGTADAAKTG LDKISKTSRV
LMVINGDDSA FYKPETIKNI LEIHKERERK LTFVSLMKNE PTGLGRVIRG KNGLITKIVE
EKDATEEERK IKEVNDGLYV FDRSWFTENI SKVKKGPQAE YYLVDLIKIA IDQGDRMATY
TLPNDDEWHG VNTPEQLTDA QKKMEEKLSE KI
//
