ID A0A0L0LLI0_9BACT Unreviewed; 430 AA.
AC A0A0L0LLI0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:KND50988.1};
DE EC=6.3.2.10 {ECO:0000313|EMBL:KND50988.1};
GN Name=murF {ECO:0000313|EMBL:KND50988.1};
GN ORFNames=AB202_01095 {ECO:0000313|EMBL:KND50988.1};
OS Parcubacteria bacterium C7867-007.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659201 {ECO:0000313|EMBL:KND50988.1, ECO:0000313|Proteomes:UP000037534};
RN [1] {ECO:0000313|EMBL:KND50988.1, ECO:0000313|Proteomes:UP000037534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-007 {ECO:0000313|EMBL:KND50988.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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:KND50988.1}.
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DR EMBL; LFCQ01000003; KND50988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LLI0; -.
DR STRING; 1659201.AB202_01095; -.
DR PATRIC; fig|1659201.3.peg.212; -.
DR Proteomes; UP000037534; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:KND50988.1}.
FT DOMAIN 102..212
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 270..354
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 430 AA; 46049 MW; 546966E29AC9DDD6 CRC64;
MKTLLRSIFA SVLGWLAAGI VRKYKPKIVM VTGSVGKTST KDAVAAALSG IYLVRKSDKS
YNSEFGVPLT IVGVDSPWAN PGAWLKVFGE AFALRFFPSH YPNMLVLEVG ADRPGDLAKI
MKIALPDAVV VTKLPEVPVH VEAYPTPAAV REEEFYPAYA LDEGMPLIMN AEDEYAIAMS
ARLTARTMTF GVSEHADVRI TQPKVHVEDG NIVGMEALLH IGSEEHLLTV PGTVGQPALY
APAAAIATAI ALGLTVPEAL KGLTSYAPPP GRARILNGKN GSTLIDDSYN ASPAATVEAL
ASLNLVAGER KLRRIAVLGD MLELGRYSFE EHERIGTLAA RQTDLLVTIG VRARGIAAAA
LEAGMPETSI QQFSTSEEAA PMLAELIGKG DVVLIKGSQS IRTERITEAL LSTSEDQEHL
VRQSKQWKSI
//
