ID A0A0R2UGB4_9GAMM Unreviewed; 480 AA.
AC A0A0R2UGB4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABS10_03695 {ECO:0000313|EMBL:KRO96459.1};
OS SAR86 cluster bacterium BACL1 MAG-120820-bin45.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1655612 {ECO:0000313|EMBL:KRO96459.1, ECO:0000313|Proteomes:UP000051027};
RN [1] {ECO:0000313|EMBL:KRO96459.1, ECO:0000313|Proteomes:UP000051027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL1 MAG-120820-bin45 {ECO:0000313|EMBL:KRO96459.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|RuleBase:RU004135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000256|ARBA:ARBA00005898}.
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:KRO96459.1}.
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DR EMBL; LICS01000001; KRO96459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2UGB4; -.
DR STRING; 1655612.ABS10_03695; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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-UniPathway.
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; 3.40.1390.10; MurE/MurF, N-terminal 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 InterPro; IPR035911; MurE/MurF_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; PF02875; Mur_ligase_C; 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.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU004135};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|RuleBase:RU004135};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|RuleBase:RU004135};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|RuleBase:RU004135}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|RuleBase:RU004135}.
FT DOMAIN 21..70
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 106..308
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 330..410
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 480 AA; 54044 MW; A1368DB3464A6931 CRC64;
MNSFSSIASF FQIDTQVDLA ISGITDDSRS VQGNFLFVAR PGVNCHGLTF VEDAIKNGAT
CILSDKPPPL SIKIPYIHVT NLERVLIKFL FKFYNLDENN FLFHGITGTN GKTSTAFIAH
QIMHKLGRPS CYIGTLGAFV NTNFFPTKGN STPGIFELFQ LLADHKFNEL TYIFLELSSH
ALEQNRLSSL PFTQTMLLNI YSDHLDYHLT HEEYVQAKLA ILDLPSKYPP IIHTDSAVVQ
SSLWAIEHKH QVFFLSSQDA ARPYFYKKIF KHPETSNIVF QFPSFRSTKN LSLFPEFNLD
NFACAIGLLS NSCSGSELEA LDYTDLELPP GRSEHFICSQ GHVFIDYAHD PEAMKNILSS
LAASYDELVL IFGCGGDRDK LKRPQMMRVA EEFAHEIIFT SDNNRSESFE MIAADAVGTR
QFKNLSIVKS RPDAINQGLR SLNSKNILVI LGKGHEIFME EGGKFIPFND REYILGNKNT
//
