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Database: UniProt
Entry: A0A1G7BZX9_9FLAO
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ID   A0A1G7BZX9_9FLAO        Unreviewed;       451 AA.
AC   A0A1G7BZX9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=UDP-N-acetylmuramate: L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000313|EMBL:SDE32597.1};
GN   ORFNames=SAMN05421855_101106 {ECO:0000313|EMBL:SDE32597.1};
OS   Ulvibacter litoralis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=227084 {ECO:0000313|EMBL:SDE32597.1, ECO:0000313|Proteomes:UP000199321};
RN   [1] {ECO:0000313|EMBL:SDE32597.1, ECO:0000313|Proteomes:UP000199321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16195 {ECO:0000313|EMBL:SDE32597.1,
RC   ECO:0000313|Proteomes:UP000199321};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNBA01000001; SDE32597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7BZX9; -.
DR   STRING; 227084.SAMN05421855_101106; -.
DR   OrthoDB; 9804126at2; -.
DR   Proteomes; UP000199321; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; 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; IPR036565; Mur-like_cat_sf.
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; 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.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:SDE32597.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199321}.
FT   DOMAIN          2..103
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          108..279
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   451 AA;  50718 MW;  1BBBC7856140BEFE CRC64;
     MRIHFIAIGG SAMHNLALAL HLKGDHVTGS DDEIFEPSKG RLDAKGLLPD AFGWFPEKIT
     TDIDAIILGM HAKADNPELL KAKELGLTIY SYPEFLYEQS KHKTRVVIGG SHGKTTITSM
     ILHVMHYHDR EVDYMVGAQL EGFDVMVKLT DDNDFIVLEG DEYLSSPIDR RPKFHLYKPN
     IALLSGIAWD HINVFPTYEN YVEQFDIFLN QITNGGAIIY NEEDSEVKRV VEDSTSLIKK
     YPYQTPSYTV VDGETLLDTP EGPMPIEVFG KHNLNNLEGA RWICQLMGVD AADFYEAIAT
     FKGASKRLEK IAETKTAVAY KDFAHSPSKV KATTEAVKSQ FPDRKLIACL ELHTYSSLNP
     EFLSQYKGAL DAADSAVVFY SPHAVMIKQL EEIKTEQIDA AFDRDDLIVF TNPADFKTYL
     YSQEYENTSL LLMSSGNYGG LDFDTVKEYI K
//
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