ID A0A140DU91_9FIRM Unreviewed; 440 AA.
AC A0A140DU91;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:AMK54218.1};
DE EC=6.3.2.8 {ECO:0000313|EMBL:AMK54218.1};
GN ORFNames=AALO17_10840 {ECO:0000313|EMBL:AMK54218.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK54218.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK54218.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK54218.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
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DR EMBL; CP011391; AMK54218.1; -; Genomic_DNA.
DR RefSeq; WP_067556284.1; NZ_CP011391.1.
DR AlphaFoldDB; A0A140DU91; -.
DR STRING; 1702221.AALO17_10840; -.
DR GeneID; 78477847; -.
DR KEGG; fro:AALO17_10840; -.
DR PATRIC; fig|1702221.3.peg.1046; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000069771; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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 InterPro; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445:SF3; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF51984; MurCD N-terminal domain; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AMK54218.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000069771}.
FT DOMAIN 3..101
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 106..257
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 297..368
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 440 AA; 49070 MW; F123595FFBB16CCD CRC64;
MAVHFTGIKG TGMAALAGIL KDEGFDVKGS DIDKYIFTQD ELEKRGIPVS SFDPANIHAG
DTVIAGLSFD EAHPEIQKAL ADPTVTVYWY NEYLGKLLER YESISIAGTH GKSTTTGLLA
SVLKLQAPTG FLIGDGHGSM PEHARYFILE SCEFKRHFLA YHPDYAIITN IELDHVDYYR
DMEDYVSAFQ SFADQVKKLA VVCGDDEHLV RLHYSCPYVT YGLKDGCDYQ AVNVQDDEHG
ISFDVRKDGN IIAHTALPES GYPFLIDSLG VFAMASELGM DPETIEEGLH DYQGINRRFV
IEEAGNSILI DDYAHHPTAI RYMIEAARSR YPGRKVIALY KPDRYSRLQF FLDEFAESMS
LADEAILLDF PKNAVREDDT ITVTIQDLID RVPGSIQGEV DQATAGKLAA EDGAVFLFMS
SKDIYLLRDM VRDLLEKQPG
//
