ID K2CWY9_9BACT Unreviewed; 264 AA.
AC K2CWY9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
DE Flags: Fragment;
GN ORFNames=ACD_31C00103G0001 {ECO:0000313|EMBL:EKD90206.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD90206.1};
RN [1] {ECO:0000313|EMBL:EKD90206.1}
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:EKD90206.1}.
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DR EMBL; AMFJ01012121; EKD90206.1; -; Genomic_DNA.
DR AlphaFoldDB; K2CWY9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; 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; IPR005762; MurD.
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 Pfam; PF21799; MurD-like_N; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 119..236
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT NON_TER 264
FT /evidence="ECO:0000313|EMBL:EKD90206.1"
SQ SEQUENCE 264 AA; 29814 MW; 9F56A5A5E124E79C CRC64;
MNGKFKNTKV LVFGLGVNQG GLGATKFFGK LGAKIRVTDL KTAEQLKTSL DELKDFPDIE
YILGGHREED FDWADLIIKN PAIKPGNKYL EYAKSKNKQI EMDMGIFLQY VLPSQIIGIT
GTKGKSTTST LIYEVLKTSH SRSVILAGNI GKSVLDTIEY VNPKTLVVLE LSSFQLEAFE
QHQVSPKYAV ITNIYPDHLN YYQNMEEYIL AKKIIAKYQT TENFLFLRKG DKVTNSPDFL
KNLKGQINYF SAVDLPKDFK PKLP
//
