ID W2URB7_9FLAO Unreviewed; 452 AA.
AC W2URB7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000313|EMBL:ETN96710.1};
DE EC=6.3.2.8 {ECO:0000313|EMBL:ETN96710.1};
GN ORFNames=P278_01360 {ECO:0000313|EMBL:ETN96710.1};
OS Zhouia amylolytica AD3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zhouia.
OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN96710.1, ECO:0000313|Proteomes:UP000018850};
RN [1] {ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA Jin H., Jeon C.O.;
RT "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN96710.1, ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|EMBL:ETN96710.1,
RC ECO:0000313|Proteomes:UP000018850};
RX PubMed=27151796;
RA Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT Sediment.";
RL Genome Announc. 4:0-0(2016).
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:ETN96710.1}.
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DR EMBL; AYXY01000001; ETN96710.1; -; Genomic_DNA.
DR RefSeq; WP_038260725.1; NZ_AYXY01000001.1.
DR AlphaFoldDB; W2URB7; -.
DR STRING; 376730.SAMN04487906_2221; -.
DR PATRIC; fig|1286632.3.peg.135; -.
DR eggNOG; COG0773; Bacteria.
DR Proteomes; UP000018850; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1.
DR Pfam; PF01225; Mur_ligase; 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 Ligase {ECO:0000313|EMBL:ETN96710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018850}.
FT DOMAIN 2..101
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..280
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 452 AA; 50761 MW; AF53303F5E9AC937 CRC64;
MHIHFIAIGG SAMHNLALAL LEKGYTITGS DDVIFEPSKS RLEAKGLCPE TFGWYPEKIT
SDLDAVILGM HAKEDNPELL KAQELGVKIY SYPEFLYEQS KEKTRVVIGG SHGKTTITSM
ILHVLNYHDI EVDYMVGAQL EGFDNMVHLT HDNEFIVLEG DEYLSSPIDR RPKFHLYKPN
IALLSGIAWD HINVFPTYEG YVEQFKIFVD SIVSGGSINY NEEDEEVKRV VEASENQIRK
IPYGTPEYFV EGEETYLETP EGPMPLEIFG EHNLNNLMGA KWICQHMGVD EDDFYEAIVT
FKGAAKRLEK IAESATSVAY KDFAHSPSKV AATTKAVKEQ YPNRKLIACA EFHTYSSLNS
DFLNEYKGAL DSADEAVVFY SPDAVKIKGL TEISEAQISA ALQRDDLKIF TNPDDFKSYL
FSLELDNTTL LLMSSGNYGG LNFDEVKDLI KS
//
