ID A0A0U3E9G2_9LACT Unreviewed; 458 AA.
AC A0A0U3E9G2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
GN ORFNames=NY10_2009 {ECO:0000313|EMBL:ALV22598.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22598.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV22598.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV22598.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) 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|HAMAP-Rule:MF_02019,
CC 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-L-lysine = ADP + H(+) + phosphate + UDP-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-
CC alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57822, ChEBI:CHEBI:70758,
CC ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.10;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02019};
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|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC ECO:0000256|RuleBase:RU004136}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR EMBL; CP010796; ALV22598.1; -; Genomic_DNA.
DR RefSeq; WP_058919792.1; NZ_CP010796.1.
DR AlphaFoldDB; A0A0U3E9G2; -.
DR STRING; 1564681.NY10_2009; -.
DR KEGG; carc:NY10_2009; -.
DR PATRIC; fig|1564681.3.peg.2019; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000064734; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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 HAMAP; MF_02019; MurF; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02019};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_02019};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:ALV22598.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_02019}; Reference proteome {ECO:0000313|Proteomes:UP000064734}.
FT DOMAIN 26..99
FT /note="Mur ligase N-terminal catalytic"
FT /evidence="ECO:0000259|Pfam:PF01225"
FT DOMAIN 110..295
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT DOMAIN 317..397
FT /note="Mur ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02875"
FT BINDING 112..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ SEQUENCE 458 AA; 50174 MW; A0BAB25ED35B8181 CRC64;
MFSLTVREIA SAVGAQNATD KWADVEISAV GFDTRKLFSG SLFVPLIGDN DGHAFIEKAI
ENGAKAAFWS RPLDEAPTEI PVIQVEDTLK ALQALASYYL KKIHPKVIGI TGSNGKTTTK
DMTEAVVSSA YRVHKTQGNF NNHIGLPMTI LEMPEDTEVI ILEMGMNHAD EIRVLSDLAE
PDIAIITMIG ESHIEYLGSR AGIADAKMEI ISGLKPDGVL IYPGEEPLLE ERVHSLVKEQ
LKTFGTTEKN DLYPLTIDAQ MTETTFTTNA EPDLSITLPV LGTYNVTNAL AALSAGLVLG
ISIEQAAPKL SVFQLTKNRT EWLTGIHESM ILNDAYNANP TAMKLVLTNF SALPNTGRKI
VVLGDMLELG QQSRELHKSI EEVLSAESID QVFLYGNEMH VLYAALLGKF AEGHLHYFTG
DKEPMIHQLK QLIQPKDHIL IKSSLGTDLL TVVQELKV
//
