ID   K1Z2W2_9BACT            Unreviewed;       434 AA.
AC   K1Z2W2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACD_63C00125G0008 {ECO:0000313|EMBL:EKD49490.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD49490.1};
RN   [1] {ECO:0000313|EMBL:EKD49490.1}
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:EKD49490.1}.
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DR   EMBL; AMFJ01026623; EKD49490.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1Z2W2; -.
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; 3.90.190.20; 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; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   Pfam; PF02875; Mur_ligase_C; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        69..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          98..255
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          277..358
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
SQ   SEQUENCE   434 AA;  48693 MW;  54E307FBB91FAE49 CRC64;
     MMDFFKKIVE KILRALSINL LKKHDPFIVG VSGSIGKTST KEAIYTVLKK EFYTRESDKN
     YNNELGVPLT ILGLGTVGRS FLLWVGVFFK AILKILFEKK YPKILVLELG VDRPKDMDFL
     MSFVSPRIGV VTSVGPTHLE FFRSVKDIAD EKAKLIEALS YNGIAILNFD DEKVRDMRDK
     TEAKVMTYGL KEGADVRGIL TESSLSFDAD RWLNMAQRDR FATVFKVGYQ GTVVPVRLKS
     VGAPHIYAVL AAIVTGLAMD INLVQITKSL LDYEPPHGRM NLIEGIKKTL IIDDTYNSAP
     DSAIAAVSYL DKIQTSGRKI AIMGDMLELG IYTEDGHRKV GRALVKFVDI LVTVGEKSKF
     MAEEARGEGL ADVYEFDTNE KVGDFIQKKL NKFDVVLVKA SQGIRLEKVV KEIMAEPLKA
     ESMLVRQDEK WERV
//