ID D2MN67_9FIRM Unreviewed; 523 AA.
AC D2MN67;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000313|EMBL:EFC05889.1};
DE EC=6.3.2.10 {ECO:0000313|EMBL:EFC05889.1};
GN Name=murF {ECO:0000313|EMBL:EFC05889.1};
GN ORFNames=HMPREF9013_0084 {ECO:0000313|EMBL:EFC05889.1};
OS Bulleidia extructa W1219.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Bulleidia.
OX NCBI_TaxID=679192 {ECO:0000313|EMBL:EFC05889.1, ECO:0000313|Proteomes:UP000005017};
RN [1] {ECO:0000313|Proteomes:UP000005017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1219 {ECO:0000313|Proteomes:UP000005017};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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:EFC05889.1}.
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DR EMBL; ADFR01000003; EFC05889.1; -; Genomic_DNA.
DR RefSeq; WP_006626838.1; NZ_ADFR01000003.1.
DR AlphaFoldDB; D2MN67; -.
DR STRING; 679192.HMPREF9013_0084; -.
DR eggNOG; COG0770; Bacteria.
DR OrthoDB; 9801978at2; -.
DR Proteomes; UP000005017; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 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:EFC05889.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005017};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..371
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 391..468
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 523 AA; 61025 MW; 60879FE70136F20D CRC64;
MIWIGLEAVL FFFGFYLEFQ YVLHMFQQNR YEIHRFYHWM SDQRKEIQEE LWFPFGVAII
GVFWAFIPNL SIKWIGLMAL SFLVMVMNHF QNQFHITIKP LVFTARVKRQ LFISAWLVGV
TIFSLIYFQL DYLWLLCLVF TPWLFMYVVG WMTWPFEKML QQYYIHLGKK RLYAQRDLIK
IGITGSYGKT STKNIIQSIV REEYHSLMTP ASYNTPMGIT MTIRNYLKPI HQVFVCEMGA
DHVGEITRLM KYVQPQIGVV TSVGPQHLLT FGSLENIIHE KMQMIERLPK DGLGVINLDN
DYIRQYRVKN SVPLISFGIQ SEDVDYRAVK ISYTTTGSYF TVVHAKEEVA FHTKLLGELN
IMNILSGIVV ARHLGISWKS LQRAVANMEQ VEHRLELKKI NGHRFIDDAF NANPIGAKMA
LEVLSMMPGK RYIITPGMID LGKKQDEYNR EFGKRMKHFV DEVILVGPKQ TKAIQEGLAE
MNFDADHIHV YQTVQEALAY VYEHADEHDT ILLENDLPEA FSR
//
