ID A0A1E3LWF0_9SPHN Unreviewed; 465 AA.
AC A0A1E3LWF0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:ODP38069.1};
GN ORFNames=BFL28_15705 {ECO:0000313|EMBL:ODP38069.1};
OS Sphingomonas turrisvirgatae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP38069.1, ECO:0000313|Proteomes:UP000094487};
RN [1] {ECO:0000313|EMBL:ODP38069.1, ECO:0000313|Proteomes:UP000094487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCT13 {ECO:0000313|EMBL:ODP38069.1,
RC ECO:0000313|Proteomes:UP000094487};
RA D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
RL Submitted (AUG-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:ODP38069.1}.
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DR EMBL; MDDS01000020; ODP38069.1; -; Genomic_DNA.
DR RefSeq; WP_069320214.1; NZ_MDDS01000020.1.
DR AlphaFoldDB; A0A1E3LWF0; -.
DR STRING; 1888892.BFL28_15705; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000094487; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:ODP38069.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000094487}.
FT DOMAIN 9..108
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 115..293
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 314..368
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 465 AA; 48723 MW; 6387DA61B979BD4A CRC64;
MHNGKPHFFV GIGGSGMMPL AMILAGQGAK VAGSDRSLDS GRLPAKFDAL RALGIDMFAQ
DGSGIVSPEQ VVVASAAVEA SVPDMVRAAD LGCPRLTRAE LNARLFNAAR MSIGIAGTSG
KSTVTGMIAW ILHSLGRDPT VMNGAVMKNF ASPDAPFASA LVGGDELYVS EVDESDGSIA
LYSPHVAVLN NISLDHKSLD ELRALFGDFA AKARATIVNV GDAESAALAT ALDRSRTTTF
AVEGEADLSA RNLSPEAFAM RFDLVTADAT LPVRLAVPGA HNVANALAAI GAVTAAGIAL
PDAVRAIEGF TGLRRRFEWV GEAGGVAVID DFGHNPDKIG ATLDTLHAFP GRVLAFFQPH
GFGPLKVMRR EMVEMFVNKL RPDDRLVLSD PVYQGGTVNR EVTSGDIVTD IAASGRNARH
IPDRDAAAAH LVAQAQPGDR IVVMGARDDT LSQLAASMLS LLERR
//