ID E8V5L5_TERSS Unreviewed; 481 AA.
AC E8V5L5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=UDP-N-acetylmuramate {ECO:0000313|EMBL:ADV81549.1};
GN OrderedLocusNames=AciPR4_0716 {ECO:0000313|EMBL:ADV81549.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV81549.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV81549.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
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DR EMBL; CP002467; ADV81549.1; -; Genomic_DNA.
DR RefSeq; WP_013567282.1; NC_014963.1.
DR AlphaFoldDB; E8V5L5; -.
DR STRING; 401053.AciPR4_0716; -.
DR KEGG; tsa:AciPR4_0716; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_0_2_0; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000006844; Chromosome.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR005757; Mpl.
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 NCBIfam; TIGR01081; mpl; 1.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT DOMAIN 6..99
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 112..303
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 323..389
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 481 AA; 52404 MW; 0D37BF99E60DC52D CRC64;
MRETKHVHLI GICGTAMASL AGMLQAQGHR VTGSDAAAYP PMSDQLAEMH IPVMQPYSEA
NLTPRPDMVV VGNAISRGNP ELEYVLDQRV CFVSMAALIH DEFLQEREPL VVCGTHGKTT
TTSMLAWIYE VASRTMPELA ASFLIGGVAE NFGTSFLVRL ETKPFILEGD EYDTAFFDKG
PKFLHYFPDA AILTHVEYDH ADIYADLEAV KTAFKRLVNL VPRRGRIVAF DGSANVTECV
ARAFCAVERY GFEPSSYWQM KDFKGGASTK WTLLREGKHF ADLELPMAGE HNALNATAAA
AMAAGQGVPA VAIVEALASF RSVKRRLEVR AEVNGITIID DFAHHPTAIR ETLRALRSAY
PDRRLIAVLE PRSNTLRRNV FEADLIDSLS GANEVALASV FKSEAIPTTE RLEPQRVVAG
LTQIGIPAQL YSDADAIVTG LTPRLLPGDV VAILSNGGFG DIYTKLPRAI AAQNSEAENG
E
//
