ID A0A1M3G1E9_9SPHI Unreviewed; 456 AA.
AC A0A1M3G1E9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:OJW33680.1};
GN ORFNames=BGO54_10610 {ECO:0000313|EMBL:OJW33680.1};
OS Sphingobacteriales bacterium 46-32.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW33680.1, ECO:0000313|Proteomes:UP000184358};
RN [1] {ECO:0000313|EMBL:OJW33680.1, ECO:0000313|Proteomes:UP000184358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46-32 {ECO:0000313|EMBL:OJW33680.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJW33680.1}.
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DR EMBL; MKTY01000019; OJW33680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3G1E9; -.
DR STRING; 1895839.BGO54_10610; -.
DR Proteomes; UP000184358; 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; 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:OJW33680.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 13..113
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 118..287
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 309..384
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 456 AA; 49280 MW; C0793E38A482577D CRC64;
MIQDIKDFKQ PFFIGVAGTG MSALAQYLQG TGKRVTGSDR FFQDGVYNAT QDKLESAGIR
CYVQDGRGIT EHTDLVVVST AVEDTVPEVQ KARQLGIPII RRSELLAVIA ASKKTIAVGG
TSGKSTTSAM LFDILRYAGM QPSIISGAGL VSLMKEGAIG NAFTGQGEWL VIEADESDGS
IVQYKPEIGL LLNVDKDHKE LDVLMDVFAV FKNNSKHFVV NQSHPLAAQL SQDLTHDFSV
NGPGGYVATD FVQQGLQISF RINQVPFELQ LAGAHNMENA LAASAVAAML GVPLATAAAA
LAGYEGIYRR HQVLGRKGDI WVIDDYAHNP VKCAAAIHAC QPIAPKVIAW FQPHGYGPTK
FLRHDFVEEI GKALRPEDEI WMSEIFYAGG TAVKDISSGD LIADLQSAGK SAFFVADRNK
LLETIRPHLT GSCVLLLMGA RDPSLEDFAK QVWDSL
//