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Database: UniProt
Entry: A0A1G6XUA4_9ACTN
LinkDB: A0A1G6XUA4_9ACTN
Original site: A0A1G6XUA4_9ACTN 
ID   A0A1G6XUA4_9ACTN        Unreviewed;       430 AA.
AC   A0A1G6XUA4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000313|EMBL:SDD81758.1};
GN   ORFNames=SAMN05421872_11190 {ECO:0000313|EMBL:SDD81758.1};
OS   Nocardioides lianchengensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1045774 {ECO:0000313|EMBL:SDD81758.1, ECO:0000313|Proteomes:UP000199034};
RN   [1] {ECO:0000313|EMBL:SDD81758.1, ECO:0000313|Proteomes:UP000199034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6858 {ECO:0000313|EMBL:SDD81758.1,
RC   ECO:0000313|Proteomes:UP000199034};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; FMZM01000011; SDD81758.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6XUA4; -.
DR   STRING; 1045774.SAMN05421872_11190; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199034; 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:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR036565; Mur-like_cat_sf.
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; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:SDD81758.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199034}.
FT   DOMAIN          111..222
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   430 AA;  44058 MW;  0236FA0B19E6B683 CRC64;
     MIGAGTGWRG LAGLRVGVWG VGVEGSASLR RLAADGVTPY AVVDRVAGDG VLALDAGGLD
     RLLECDVVVK SPGISPYDEP ARTLTAAGVR LAGGLGLWLE DAPRDRVACL TGTKGKSTAT
     AIAGALATGL GSRAFVGGNI GRAPWEPGVE EADVYLVETS SYQAHDVTTG PRVVAVTSLS
     QDHLVWHHGY DGYVRDKLSL CTRPGVETVV APAADAELER YADLLGPHVL RVAEAPAPWA
     DGLGLIGRHN LRNALLAQAV LAALGVPGAE DEGALAAAAA SYTPLPSRLT RVGAVGDVEF
     VDDSLSTNTL PTLAAVASFP GRRVALLVGG QDRGIDYAPL AAGLADVPDL LVLTLPDNGP
     RIASTIRAVA PGVPVEECPD LASAVRRGHA FAAPDGVVLL SPAAPSFGVF RDYAERAEVF
     TAAMRALPHG
//
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