ID W0ALG7_9SPHN Unreviewed; 466 AA.
AC W0ALG7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=UDP-N-acetylmuramate--alanine ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=NX02_24390 {ECO:0000313|EMBL:AHE56485.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE56485.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE56485.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE56485.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP006644; AHE56485.1; -; Genomic_DNA.
DR RefSeq; WP_025294595.1; NZ_CP006644.1.
DR AlphaFoldDB; W0ALG7; -.
DR STRING; 1123269.NX02_24390; -.
DR KEGG; ssan:NX02_24390; -.
DR PATRIC; fig|1123269.5.peg.4776; -.
DR eggNOG; COG0773; Bacteria.
DR HOGENOM; CLU_028104_2_1_5; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000018851; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000018851}.
FT DOMAIN 9..107
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 115..292
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 313..364
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 466 AA; 47822 MW; F97D13B78EA5A8EB CRC64;
MIGGKSFFFI GIGGSGMLPL ASILRARGNT VAGSDRSLDQ EGAGAKFDYL RAQGIALFPQ
DGSGVVSADQ IVVASAAIEH GVPDMVAARE VGALRLSRAE LLASLFNDSP NGVGVAGTSG
KSTVTGMIAW ILHATGHAPT VMNGAVMKNF VTGDAPFASA LVGDGDVFVS EVDESDGSIA
LYRPDVAVVG NVSLDHKPLE ELRQLFGDFL HHAKTAVVNL DNADSAGLAD GHASVITYGI
DQPTAALSAS AIVEHPFSID FTLNANGRAI PVALQVPGRH NVANALAAIG AATALGLTAE
QAAAALGGFV GLRRRFDLVG EAAGVAVIDD FGHNPDKIAA TLATLHAFPG RLLLLFQPHG
YGPLKVMREA LIDCFATNMA ADDLLLMPDP VYRGGTVDRA VGSADIVDGI VSAGRDARHV
ADRDACAATL VEMARPGDRI VVMGARDDSL PAFAAGIVDA LGRRAA
//
