ID A0A0G1KZW9_9BACT Unreviewed; 414 AA.
AC A0A0G1KZW9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=UDP-N-acetylmuramoylalanine-D-glutamate ligase {ECO:0000313|EMBL:KKT53444.1};
DE Flags: Fragment;
GN ORFNames=UW45_C0032G0013 {ECO:0000313|EMBL:KKT53444.1};
OS Parcubacteria group bacterium GW2011_GWC2_44_22.
OC Bacteria.
OX NCBI_TaxID=1618930 {ECO:0000313|EMBL:KKT53444.1, ECO:0000313|Proteomes:UP000034136};
RN [1] {ECO:0000313|EMBL:KKT53444.1, ECO:0000313|Proteomes:UP000034136}
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|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KKT53444.1}.
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DR EMBL; LCII01000032; KKT53444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KZW9; -.
DR Proteomes; UP000034136; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
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; 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; IPR005762; MurD.
DR PANTHER; PTHR43692; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR PANTHER; PTHR43692:SF1; UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF21799; MurD-like_N; 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; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKT53444.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 140..298
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 337..407
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT NON_TER 414
FT /evidence="ECO:0000313|EMBL:KKT53444.1"
SQ SEQUENCE 414 AA; 45484 MW; 9155043F5E1FAFBB CRC64;
MSKKIKKQFL PTTGQKVVVM GLGLHGGGVA TAAFFAKSGA TVIATDLKSA DDLALSLEKL
RKFKNIEYVL GRHRASDFSD ADLIIRNPAV QNDAPLLQLA RKNNIPVHTD ISFFLNLLRN
LTCLAGRQEL EIKNFPVIGI TGTKGKSTTA ALLHHVLTKC GQQTLLAGNI CKSPLNFVKI
NSKNWKLEIP ARQQLELQAI AGGENWKFII LELSSWQLES LGEHRLSPKL ALITNILPDH
LNRYQNFAAY VQAKKLIYKY QTNKDALFLN SADPRLRQIG ASPSIKAKIV WYGASGKDGS
LSLIHPNNLS AVKSVCRYLK IPARPMEKAI KSFPGLNGRL EHLGIINGIT YINDTCATQP
EATIYAIDKL SGKKIILIAG GEDKKLDFTE LARTIAKKVK TLVLFKGSAS DKIL
//
