ID A0A1F6V8W5_9BACT Unreviewed; 448 AA.
AC A0A1F6V8W5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|RuleBase:RU003664};
DE EC=6.3.2.9 {ECO:0000256|RuleBase:RU003664};
GN ORFNames=A2647_00040 {ECO:0000313|EMBL:OGI66107.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_40_24b.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801739 {ECO:0000313|EMBL:OGI66107.1, ECO:0000313|Proteomes:UP000177370};
RN [1] {ECO:0000313|EMBL:OGI66107.1, ECO:0000313|Proteomes:UP000177370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC {ECO:0000256|RuleBase:RU003664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC Evidence={ECO:0000256|RuleBase:RU003664};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|RuleBase:RU003664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003664}.
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:OGI66107.1}.
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DR EMBL; MFTP01000004; OGI66107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6V8W5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000177370; 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:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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 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; IPR005762; MurD.
DR NCBIfam; TIGR01087; murD; 1.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|RuleBase:RU003664};
KW Cell division {ECO:0000256|RuleBase:RU003664};
KW Cell shape {ECO:0000256|RuleBase:RU003664};
KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU003664};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OGI66107.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU003664}.
FT DOMAIN 122..232
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 301..377
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 448 AA; 50551 MW; E38FBF56807FD4F8 CRC64;
MTDYKKFFKN KKVTVMGLGV LGRGVGDTVF LAECGAKLLV TDLRTKEQLK ESIGKLKKFK
NIKYVLGRHR LEDFRNADLI LKNPAIPLHS IYIKEARKNR IPVEMSATLF SKLSSLPIIA
MTGTRGKSTT THLIYHILKY GGKKVILGGN IRGVSNLQLL KVARHAKIAV LELDSWQLQG
FGDARISPNI SVFTTFFPDH MGYYKGSMKK YFSDKSHIFN HHTKDDLLIV GKQALPFIKK
WGGKIRSKMI VPEGRLPKGW KSNLIGLHNE YNARLAVEVA RSLSIPNAKI KKALTTFVPL
SGRLQFLRSV RGIKIYNDNS STTPDATIAA LRAVGDLKVK KVVLIIGGDN KFLDMSGLLA
EIPKFCSKVV LFKERGTDTI QEKIFEFRKR GIEVYEEEGL QNTVKRAFSI AKRRETILYS
PAFFSFGKHF KNEFDRGDQF VKLVKGLK
//
