ID J5KHE3_9GAMM Unreviewed; 445 AA.
AC J5KHE3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=NT02SARS_0325 {ECO:0000313|EMBL:EJP73718.1};
OS SAR86 cluster bacterium SAR86B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1123867 {ECO:0000313|EMBL:EJP73718.1, ECO:0000313|Proteomes:UP000010116};
RN [1] {ECO:0000313|EMBL:EJP73718.1, ECO:0000313|Proteomes:UP000010116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT lineage.";
RL ISME J. 6:1186-1199(2012).
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}.
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DR EMBL; JH611165; EJP73718.1; -; Genomic_DNA.
DR AlphaFoldDB; J5KHE3; -.
DR HOGENOM; CLU_031507_1_2_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010116; 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; IPR000713; Mur_ligase_N.
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; 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 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EJP73718.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|RuleBase:RU004136};
KW Reference proteome {ECO:0000313|Proteomes:UP000010116}.
FT DOMAIN 24..99
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 108..294
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 317..388
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
SQ SEQUENCE 445 AA; 50181 MW; 6A6B342722CB19F6 CRC64;
MLLIESTFEL AKLSEEEIKT RSRIKNFVID SRQVKKNSVF IALKGNNLDG NDFIYDALEK
GACLAVTDNK NFKEDANKNI LYVNDTYKFL LKTSQNLAEN FNGIKIGITG SNGKTSTTQI
LSHVIKFSSS TIKNFNNEIG MLLSILDTKY DSKVLVIEMG ARKLGDIDFL SSILKPHIGI
ITNIGNSHIE NLKNLDGVLK VKSELVNNIV KNGSLIVPGD NNRHLNFWKS LRKDITVFSF
GLENTNHYYP KEMASNLDGL SFNIKNNISG KSIKINSKLI GDHNILNILA TYAAIIAGSL
DENYFVKSIE DFQNPERQKI MDWINGCILF NDSYNANPES MKSAIKTICK SEKRKIVIFG
DMFELGKDEV YLHQEVGEYA KIEGVDIFIG FGKLAKHAVN SFGKNSKFFE NEDELKKYII
DNIKNTDIVL LKGSRGMYME RFLNV
//
