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Database: UniProt
Entry: A0A1M3G1E9_9SPHI
LinkDB: A0A1M3G1E9_9SPHI
Original site: A0A1M3G1E9_9SPHI 
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
//
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