ID A0A0T5ZM10_9CHLR Unreviewed; 500 AA.
AC A0A0T5ZM10;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=UDP-N-acetylmuramate--L-alanine ligase, UDP-N-acetylmuramate--alanine ligase {ECO:0000313|EMBL:KRT63835.1};
DE EC=6.3.2.8 {ECO:0000313|EMBL:KRT63835.1};
GN ORFNames=XU10_C0007G0095 {ECO:0000313|EMBL:KRT63835.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63835.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT63835.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63835.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT63835.1}.
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DR EMBL; LDXM01000007; KRT63835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZM10; -.
DR STRING; 1640513.XU10_C0007G0095; -.
DR PATRIC; fig|1640513.3.peg.900; -.
DR Proteomes; UP000051896; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC.
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:KRT63835.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 26..132
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 140..332
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 352..428
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 500 AA; 50341 MW; 6A021E45D2A7D1E6 CRC64;
MTRSAAEVGR GLAAAREARP IAPGERIHVV GAAGAGASAA LLLAARAGAD ASGCDPAAPS
PYTAAAEAAG LPLARAHDPA HVAHDGGPAA DRLAVTKALT AIAPDHPELA TARRLGIPVE
AWQQVIADVA ATRDGRLVAV AGTHGKSTSA GWLMHVLADA GHDPSGFVGA LLPATLSGGI
PATARWGGGD TFLVEADEYA GNFAPYRPSL AVLLNAEWDH PDVFADEAAV LDAFEAWIRA
MVAGTDGGPP TLVANVGDPG AARVVERLGD WPGRVVRVAL DGVVDIRGRL VAGEGGRGRL
VVEGLSGGSL EAALPLPGGH NAANALAVVA AADVLGVPGQ TIAAGLASFP GVGRRLELKG
EPRGVAVLDD YAHHPTAIAA TIEAVRARYP GRRLWAVCEP LTYHRTAAML DAFAGALARA
DRAVVADIWA GRDPDTTITS AAALAAAITA RAPAPALAPG SVEATAELLA GEVRPGDVVL
VMGGGRSYVV AERLLRLLGG
//
