ID A0A1M5RLB0_9FLAO Unreviewed; 450 AA.
AC A0A1M5RLB0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=UDP-N-acetylmuramate: L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000313|EMBL:SHH26926.1};
GN ORFNames=SAMN05444148_1618 {ECO:0000313|EMBL:SHH26926.1};
OS Winogradskyella jejuensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1089305 {ECO:0000313|EMBL:SHH26926.1, ECO:0000313|Proteomes:UP000184522};
RN [1] {ECO:0000313|EMBL:SHH26926.1, ECO:0000313|Proteomes:UP000184522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25330 {ECO:0000313|EMBL:SHH26926.1,
RC ECO:0000313|Proteomes:UP000184522};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQWS01000002; SHH26926.1; -; Genomic_DNA.
DR RefSeq; WP_073085319.1; NZ_FQWS01000002.1.
DR AlphaFoldDB; A0A1M5RLB0; -.
DR STRING; 1089305.SAMN05444148_1618; -.
DR OrthoDB; 9804126at2; -.
DR Proteomes; UP000184522; 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: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: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; 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:SHH26926.1}.
FT DOMAIN 3..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 450 AA; 50861 MW; 8FB4F09252FAEA28 CRC64;
MNVHFIAIGG AAMHNLAIAL HNKGYKVTGS DDTIFDPSKS RLEAKYLLPE EFGWFPEKIT
SDLDAIVLGM HAKADNPELL KAQELGLKIY SYPEFLYEQS KDKTRVVIGG SHGKTTITSM
ILHVMHYHDR DVDYMVGAQL EGFDVMVKLT EDNDFIVLEG DEYLSSPIDR RPKFHLYKPN
IALLSGIAWD HINVFPTYEN YVEQFSIFVD SIVRGGSINY NEEDAEVKRV VQASENQIRK
LPYQTPEYTV EDGETLLETP EGPMPIEVFG AHNLNNLAGA KWICQHMGID EDDFYEAIST
FKGASKRLEK IAESKTAVAY KDFAHSPSKV KATTEAVKVQ YKDKELLACL ELHTYSSLNA
EFLKEYKGAL DTADKAVVFY SPHAVEIKKL EEVSHQQIAD AFERDDLIIY TNPQDFKDFL
FSQNFENKAL LLMSSGNYGG LDFDEVKGLF
//
