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Database: UniProt
Entry: K2AK85_9BACT
LinkDB: K2AK85_9BACT
Original site: K2AK85_9BACT 
ID   K2AK85_9BACT            Unreviewed;       444 AA.
AC   K2AK85;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Mur ligase central domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=ACD_52C00312G0001 {ECO:0000313|EMBL:EKD62077.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD62077.1};
RN   [1] {ECO:0000313|EMBL:EKD62077.1}
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:EKD62077.1}.
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DR   EMBL; AMFJ01022754; EKD62077.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2AK85; -.
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;
FT   DOMAIN          153..255
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          282..359
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKD62077.1"
SQ   SEQUENCE   444 AA;  49526 MW;  D38F9E2E773D8173 CRC64;
     CLRLAARIQL FKIRPQIVGL TGSVGKTSLR NAITAVLSGT YRVKYSKKAN SETGIPLDLL
     DLHPRDYSLG DWVRLGLSVP IQLLVNWKKY DVYVVELGID DPFPPKNMEY LLRFIKPDIG
     VFLNVAPVHT EQFSKLLPSD VVVSPKQKTR LILQAIALEK GKIITRLPAD KIAVVNRDDV
     LVWKQAQKTK ARVVTFGKQD QSKVIIKSVT HQFAAKNRLR PQDVQTHLEF RYQGHTYGLS
     LPLLVPDYYA STLAAALTVG LQMGITMEKI LMALGERFVL PPGRMSLFAG THQSLIIDSS
     YNASKQSTLG TLELLSKIPQ KPKVVVLGDM RELGAVAGSE HGIVAKKILA VADQVILIGP
     LTRKYVLSVV SPKLPTRWFA NSWEAAAWLK KKLKAGSVVL VKGSQNMIFT EVVVEQLLAY
     SQDKNSLCRR GRYWNEQRQK SRLA
//
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