ID A0A0F2J7Z5_9BACT Unreviewed; 544 AA.
AC A0A0F2J7Z5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000313|EMBL:KJR43540.1};
GN ORFNames=MCHI_000562 {ECO:0000313|EMBL:KJR43540.1};
OS Candidatus Magnetoovum chiemensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetoovum.
OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR43540.1, ECO:0000313|Proteomes:UP000033718};
RN [1] {ECO:0000313|EMBL:KJR43540.1, ECO:0000313|Proteomes:UP000033718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR43540.1,
RC ECO:0000313|Proteomes:UP000033718};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJR43540.1}.
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DR EMBL; JZJI01000161; KJR43540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2J7Z5; -.
DR PATRIC; fig|1609970.3.peg.630; -.
DR Proteomes; UP000033718; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KJR43540.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000033718}.
FT DOMAIN 14..148
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 155..377
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 397..447
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 544 AA; 60834 MW; 4CA8CA54A5F1B6B7 CRC64;
MDLKFNFIPK DVKKIHLIAA CGTGMGALAC MLQDMGFEVT GSDQNIYPPM SDFLIQKGVK
LFKGFSPSNL ILPNLSSKPV PPDSDSLNKD YSENNNYFDS SNINHSNYPD LVIIGNAVTK
NNVEAAAVME KNIPYCSMPQ ALNHFIAEDK KILLVTGTHG KTTTSSILAY ILNQAGLDPS
FMIGGIVKEF ESNYRVGKGS YIVIEGDEYD TAFFDKSSKF MHYSPYIAIL TSVEFDHADI
FKDIDHVKDV FRKFIAKMPK DSLLIASGED ADIKEIISSA LCTVQYYGRH SENSLSYSSF
SVQDGFADFS VKLKDIAAKS NNNDLQEDEI VKYTIKQNEL IKDEFKKENL KENELKVITP
IMGMHNAMNI TAVIGAAKNI GIDNQTILQA LKSFKGVKRR QDIRGVKNGI TVMDDFAHHP
SAVRETIAGV KPFFKNSRLV AVFEPRTNSS MRDIFQNDYP KSFDGADIVC IRKPSMLSKV
PEQNRIDTEK LVKDIVKQGI QAFYFEETDT IIDFLVKESK SGDLILIMSN GGFDNIHKRL
LEKL
//
