ID   A0A1V4IA68_9FIRM        Unreviewed;       468 AA.
AC   A0A1V4IA68;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:OPJ56813.1};
DE            EC=6.3.2.10 {ECO:0000313|EMBL:OPJ56813.1};
GN   Name=murF_1 {ECO:0000313|EMBL:OPJ56813.1};
GN   ORFNames=CLOTH_00950 {ECO:0000313|EMBL:OPJ56813.1};
OS   [Clostridium] thermoalcaliphilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=29349 {ECO:0000313|EMBL:OPJ56813.1, ECO:0000313|Proteomes:UP000190140};
RN   [1] {ECO:0000313|EMBL:OPJ56813.1, ECO:0000313|Proteomes:UP000190140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7309 {ECO:0000313|EMBL:OPJ56813.1,
RC   ECO:0000313|Proteomes:UP000190140};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium thermoalcaliphilum DSM 7309.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OPJ56813.1}.
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DR   EMBL; MZGW01000001; OPJ56813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4IA68; -.
DR   STRING; 29349.CLOTH_00950; -.
DR   OrthoDB; 9801978at2; -.
DR   Proteomes; UP000190140; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000313|EMBL:OPJ56813.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190140}.
FT   DOMAIN          114..300
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   468 AA;  52297 MW;  68C867150488FB9C CRC64;
     MKPFSVNQIS QIIKGNIIYW DNNKYISSFV EEFVAPKSSC LYFLLYESIN EDKLLQSLVK
     NNASGIVIRS HHKLNMQKWI DANIGIIEVD SVREAYLSSA KFYRFQFNIP FIQVVGSSGK
     TSTKDMIGYI LNESIDTLVG AKNYNAPSGV AYNIFNLDDK HKAAVLEAGM KGLGIISLSS
     DIISPSIGVI TCINSSHISN LGSMENIIKA KGEILDYLGE DSTLIINGED ENCKKLPLHK
     FKGKMLTFGF SDSNDIWASD IKYENFKTFF TANFNNMKLD CVINTFGKYY VLNSLAAIMV
     GITLGLSRCD IYRGLSKFNL PPARQELLVG INNSFIINDN FNGNPDSTKS LIMELPNISK
     DHPLILVMGD IEKDTASLEE YAVKSHFMLG EEISKLNFHR LIAVGKWAKH YIDGALNKGI
     DQEKLSYYKT VEDAQADIIN SIIPGSIILF KAHSSYVDFQ NLINKIKA
//