ID D0RN08_9PROT Unreviewed; 443 AA.
AC D0RN08;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|RuleBase:RU004136};
DE EC=6.3.2.10 {ECO:0000256|RuleBase:RU004136};
GN ORFNames=HIMB114_00001740 {ECO:0000313|EMBL:EMH79803.1};
OS alpha proteobacterium HIMB114.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=684719 {ECO:0000313|EMBL:EMH79803.1, ECO:0000313|Proteomes:UP000033990};
RN [1] {ECO:0000313|EMBL:EMH79803.1, ECO:0000313|Proteomes:UP000033990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79803.1,
RC ECO:0000313|Proteomes:UP000033990};
RA Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EMH79803.1, ECO:0000313|Proteomes:UP000033990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79803.1,
RC ECO:0000313|Proteomes:UP000033990};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC murein. {ECO:0000256|RuleBase:RU004136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC ChEBI:CHEBI:456216; EC=6.3.2.10;
CC Evidence={ECO:0000256|RuleBase:RU004136};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|RuleBase:RU004136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004136}.
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:EMH79803.1}.
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DR EMBL; ADAC02000001; EMH79803.1; -; Genomic_DNA.
DR AlphaFoldDB; D0RN08; -.
DR STRING; 684719.HIMB114_00001740; -.
DR eggNOG; COG0770; Bacteria.
DR OrthoDB; 9800958at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-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-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; IPR035911; MurE/MurF_N.
DR InterPro; IPR005863; UDP-N-AcMur_synth.
DR NCBIfam; TIGR01143; murF; 1.
DR PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE 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 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU004136};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|RuleBase:RU004136};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|RuleBase:RU004136};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|RuleBase:RU004136}; Ligase {ECO:0000313|EMBL:EMH79803.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|RuleBase:RU004136};
KW Reference proteome {ECO:0000313|Proteomes:UP000033990}.
FT DOMAIN 100..284
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 306..388
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 443 AA; 50933 MW; 4E825DBE15E81088 CRC64;
MKFNITNKIL KKKFYIDSRL VKENSVFLCI KGPNNDGHKY AKLVLDRFKR TIIICEKNSI
YLKNLKNSNR VIFCNSTKDF LINLARIKRY LLNSKNFIGI TGSSGKTSLK DLLFTVLNKY
KKSYKSQKSY NNNIGLPYTL VNQNINSEFN IYELGMNNFG EIDSLSNILK PNLAIITNIG
EAHLGNLGSI KNIAKAKAEI IKNITKQGTI ILNHDCKFFN QLKKISKKNK IKVLSFGSTS
KATVSYKVIS LNEIEIKLNN LKFKLKLNDI NPNMINNMLV CILVLSFFKL NIRKSKNYFN
KIKNTRGRGN IVKFRKEIII IDDSYNSNPS SLKSSINQFE KLSTKKKKIL VIGDMLELGK
FSKKKHGEIG NYLSKMGFNR ILLVGKDSKE IYKKIKSTFW CKYFENINIF SKYFKNVLIE
NSIIMFKASN GVGLNKLLNK KIY
//
