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Database: UniProt
Entry: K2BIC2_9BACT
LinkDB: K2BIC2_9BACT
Original site: K2BIC2_9BACT 
ID   K2BIC2_9BACT            Unreviewed;       262 AA.
AC   K2BIC2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=L-alanyl-diaminopimelate ligase {ECO:0000313|EMBL:EKD80175.1};
DE   Flags: Fragment;
GN   ORFNames=ACD_40C00190G0007 {ECO:0000313|EMBL:EKD80175.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD80175.1};
RN   [1] {ECO:0000313|EMBL:EKD80175.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD80175.1}.
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DR   EMBL; AMFJ01016736; EKD80175.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2BIC2; -.
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; 3.40.1190.10; 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; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 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.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EKD80175.1}.
FT   DOMAIN          6..94
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          102..241
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   NON_TER         262
FT                   /evidence="ECO:0000313|EMBL:EKD80175.1"
SQ   SEQUENCE   262 AA;  27856 MW;  A23E6B92313D4ADB CRC64;
     MDSKHAYFIG IKGVGMTSLA LAMADAGWSI SGSDTSETFI TDETLASHHL GVDPLSAPIP
     KGTDLIVYSS AYSPPTTINH LRSIPLAQAL AEFVQNRQVI AVAGVGGKTT TSAMLAALFH
     AAGRHVGYYV GTSSIAGLPK PGHAGTDPVY IVEADEYAIS KTDHRPKFSL ITPGILITTN
     IIHDHPDIYP TIKDTLVAFT NLIKSIPVGG TWICNPSDPL TAQIITLQGQ TLQAIKVVPY
     GSDHPLFNQL KLSVFGDQNR LD
//
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