ID A0A239KJM1_9BACT Unreviewed; 474 AA.
AC A0A239KJM1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000313|EMBL:SNT18577.1};
GN ORFNames=SAMN05421770_10520 {ECO:0000313|EMBL:SNT18577.1};
OS Granulicella rosea.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474952 {ECO:0000313|EMBL:SNT18577.1, ECO:0000313|Proteomes:UP000198356};
RN [1] {ECO:0000313|EMBL:SNT18577.1, ECO:0000313|Proteomes:UP000198356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18704 {ECO:0000313|EMBL:SNT18577.1,
RC ECO:0000313|Proteomes:UP000198356};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FZOU01000005; SNT18577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239KJM1; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000198356; Unassembled WGS sequence.
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, ECO:0000313|EMBL:SNT18577.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000198356}.
FT DOMAIN 5..99
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 111..302
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 322..400
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 474 AA; 51135 MW; 9AAD7B25E3977EDB CRC64;
MQSKHIHLIG ICGTAMASLA GMLQAQGHRV TGSDAAAYPP MSDQLAAMKI PVHEPYAEAN
LAQRPDLVVV GNAISRGNVE LEYVLDTRIP FCSMAAILHD EFLVGRESLV VAGTHGKTTT
TSMLAWIYEV ASRTDAALAP SFLIGGVAEN FGTSFHVRPT RPFLLEGDEY DTAFFDKGPK
FLHYFPDAAI LTHVEFDHAD IYEDLKAVKT AFKRFVNLIP RRGRIVAFDG AENVTECVAK
AFCAVERYGF APSSHWRVTG MTHDAHGTRW TVLRAGEHFA DLTLPMAGEH NALNATAAAA
LAAGQGVPVA AIVEALASFR SVKRRLEVRA EVGGVTVIDD FAHHPTAIRE TLRALRNAYP
GRRLWAVLEP RSNTLRRNVF EEALVESLSL ADHVVLAGVF KSENIPVHER LAPENVVARL
NEGGTPAELC ADADAIVASI APRLAAGDVV AILSNGGFGD IYHKLPAALE QVTA
//
