ID K2E9N4_9BACT Unreviewed; 254 AA.
AC K2E9N4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ACD_18C00261G0001 {ECO:0000313|EMBL:EKE06828.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE06828.1};
RN [1] {ECO:0000313|EMBL:EKE06828.1}
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:EKE06828.1}.
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DR EMBL; AMFJ01006961; EKE06828.1; -; Genomic_DNA.
DR AlphaFoldDB; K2E9N4; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..104
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 114..252
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT NON_TER 254
FT /evidence="ECO:0000313|EMBL:EKE06828.1"
SQ SEQUENCE 254 AA; 28701 MW; 3175D09A526DDDD3 CRC64;
MQKQKHIHFI GICGVAMSAL AIAFHKKGYK VTGSDKGFYP PVSTYLKEAG VPYYPGWHVE
KMTKNGDPDL VIVGNVAGSE NPEWLYVQEK KLNYKSYPEA IAEFFVKENS IVCAGTFGKT
TTTSLLAWIL QENNFDPSYM FGGISLNDMP AAKLTDSKYS ILEGDEYKSA RWDDGAKFFH
YSPTHLLLTS VVWDHADVYP TEQSYFEAFE KLLTNLPESG LLVTSERVKK EMLDFAKCKI
ITYGKDAKND YVYQ
//
