ID A0A1I4AD82_HALDA Unreviewed; 515 AA.
AC A0A1I4AD82;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000313|EMBL:SFK54120.1};
GN ORFNames=SAMN04487936_11712 {ECO:0000313|EMBL:SFK54120.1};
OS Halobacillus dabanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=240302 {ECO:0000313|EMBL:SFK54120.1, ECO:0000313|Proteomes:UP000183557};
RN [1] {ECO:0000313|EMBL:SFK54120.1, ECO:0000313|Proteomes:UP000183557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3704 {ECO:0000313|EMBL:SFK54120.1,
RC ECO:0000313|Proteomes:UP000183557};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FOSB01000017; SFK54120.1; -; Genomic_DNA.
DR RefSeq; WP_075038220.1; NZ_FOSB01000017.1.
DR AlphaFoldDB; A0A1I4AD82; -.
DR STRING; 240302.BN982_00861; -.
DR OrthoDB; 9800958at2; -.
DR Proteomes; UP000183557; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; 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; 3.40.1390.10; MurE/MurF, N-terminal 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 InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR NCBIfam; TIGR01085; murE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF08245; Mur_ligase_M; 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:SFK54120.1}.
FT DOMAIN 24..95
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 109..320
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 515 AA; 57392 MW; FC577505CDC98FFB CRC64;
MAKLKELLSS IEVLEAWNDV ELEVRGLAYN SRSVEEGDVF VCIKGFKTDG HMYVAEAVKN
GASAIVVEDY QPGWDSLPQY RVSDSRRALA ALSDAYYNHP SQSMKTVGIT ATNGKTSTSF
MADAILEEHK LKTGLIGTVV VKYGDYTEPT ELTTPESLDL HRYFAQMRDN DVSHVTMEVS
SSALDLSRVG SVDFDIVSLN NISREHIDLH GSFEEYFNSK ASLIRNAEKG KWAILNLDDP
YSASLVEETE ANLLTFSVET GDGDLICKNL DLSTGRAKFT VEIRKPIIVE DERIEPQEFT
IELSTPGYHS VYNSMVAIAV GLLNEVPIPT IQSGLKGFGG VERRFEMVFE DEFKILDDHF
ANYGNINVTL NTLQQMDYEN LKLVYAIRGS RGVTVNRENA KAIVEWAPKL GLTEVIATVS
HSHVSEKDVV TEEELRVFQE MMKEAGIHVD LYRELDDAIH HALSEVQEDD VVLLAGCQGM
DPGAQIALEQ LNKTRPDIDE EKLFKPLKNR VAGIL
//
