ID A0A0M8XG36_9ACTN Unreviewed; 472 AA.
AC A0A0M8XG36;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ADL04_07560 {ECO:0000313|EMBL:KOX05387.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOX05387.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOX05387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOX05387.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX05387.1}.
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DR EMBL; LGDZ01000074; KOX05387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8XG36; -.
DR PATRIC; fig|1519493.3.peg.1628; -.
DR Proteomes; UP000037702; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000037702}.
FT DOMAIN 12..109
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 117..300
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 323..400
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 472 AA; 48592 MW; ECB4B6C9C7B229C7 CRC64;
MSAGGPIDLS RVHFVGVGGT GMLPVARVCA ERGFTVSGSD VRVTEALKAL ARLNVRVHTG
HAAEHVPADA TAVVFTHVIG PDNPEIRAAR ALGVPVVHRS TVLNVLMAAQ PKKVAVMGTH
GKSSTAGMLA FALARLGQEP SYVVGADLDV PGSGGHAGQG SVFVAEIDES DRSHVGMNMD
VAVITNVGYD HPEVYDDEDQ VVDTYESGLA LGLREGGTVV IGIDSSGGLE LASRLVAAEN
GTGVVTFGFS TSADWRLTEV STKGRGSSAV LVGPGEVGYA LDLRTVGGHQ LLNAAAAVIT
LHVLGQDCGQ AVEQLRYFDG VVRRMTPAFE AGGVRVYDSY AHHPDEVRAD LAAARSVARE
QGRVITVFQP SGPTRLTVFG RRFGEALAGS DEVVVTGSAQ RFAVAGLETL SACIDAAGGT
CRHVEPDRAE AAVLAASLAR PGDVVVLMGP GDIAEAGQVL RTALGDTVGT AV
//
