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Database: UniProt
Entry: Q5F8G0_NEIG1
LinkDB: Q5F8G0_NEIG1
Original site: Q5F8G0_NEIG1 
ID   Q5F8G0_NEIG1            Unreviewed;       458 AA.
AC   Q5F8G0;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase {ECO:0000256|HAMAP-Rule:MF_02020};
DE            EC=6.3.2.45 {ECO:0000256|HAMAP-Rule:MF_02020};
DE   AltName: Full=Murein peptide ligase {ECO:0000256|HAMAP-Rule:MF_02020};
DE   AltName: Full=UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_02020};
GN   Name=mpl {ECO:0000256|HAMAP-Rule:MF_02020};
GN   ORFNames=NGO_0815 {ECO:0000313|EMBL:AAW89527.1};
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89527.1, ECO:0000313|Proteomes:UP000000535};
RN   [1] {ECO:0000313|Proteomes:UP000000535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-
CC       meso-diaminopimelate by linking it to UDP-N-acetylmuramate.
CC       {ECO:0000256|HAMAP-Rule:MF_02020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate +
CC         UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:29563, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:61401,
CC         ChEBI:CHEBI:70757, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC         EC=6.3.2.45; Evidence={ECO:0000256|HAMAP-Rule:MF_02020};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02020};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000256|HAMAP-Rule:MF_02020}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. Mpl subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02020}.
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DR   EMBL; AE004969; AAW89527.1; -; Genomic_DNA.
DR   RefSeq; WP_003688594.1; NC_002946.2.
DR   RefSeq; YP_207939.1; NC_002946.2.
DR   AlphaFoldDB; Q5F8G0; -.
DR   STRING; 242231.NGO_0815; -.
DR   DNASU; 3281819; -.
DR   GeneID; 66753151; -.
DR   KEGG; ngo:NGO_0815; -.
DR   PATRIC; fig|242231.10.peg.962; -.
DR   HOGENOM; CLU_028104_0_1_4; -.
DR   OMA; SGIAWDH; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000535; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106418; F:UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate 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-KW.
DR   GO; GO:0009254; P:peptidoglycan turnover; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_02020; Mpl; 1.
DR   InterPro; IPR005757; Mpl.
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   NCBIfam; TIGR01081; mpl; 1.
DR   PANTHER; PTHR43445; UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE-RELATED; 1.
DR   PANTHER; PTHR43445:SF5; UDP-N-ACETYLMURAMATE--L-ALANYL-GAMMA-D-GLUTAMYL-MESO-2,6-DIAMINOHEPTANDIOATE LIGASE; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF51984; MurCD N-terminal domain; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02020};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02020};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02020};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_02020};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02020};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02020};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02020};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_02020}; Reference proteome {ECO:0000313|Proteomes:UP000000535}.
FT   DOMAIN          3..103
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          110..301
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          321..372
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_02020"
SQ   SEQUENCE   458 AA;  49446 MW;  C90E671A963848CD CRC64;
     MKHIHIIGIG GTFMGGIAAI AKEAGFKVSG CDAKMYPPMS TQLEALGIGV HEGFDAAQLE
     EFQADIYVIG NVARRGMDVV EAILNRGLPY ISGPQWLAEN VLHHHWVLGV AGTHGKTTTA
     SMLAWVLEYA GLAPGFLIGG VPENFGVSAR LPQTPRQDPN SKSPFFVIEA DEYDTAFFDK
     RSKFVHYRPR TAVLNNLEFD HADIFADLGA IQTQFHHLVR TVPSEGLIVC NGQQQSLQDT
     LDKGCWTPVE KFGTGHGWQI GEVNADGSFD VLLDGKKAGH VAWDLMGGHN RMNALAVIAA
     ARHAGVDVQT ACEALGAFKN VKRRMEIKGT ANGITVYDDF AHHPTAIETT IQGLRQRVGG
     ARILAVLEPR SNTMKLGTMK SALPASLKEA DQVFCYAGGA DWDVAEALAP LGCRLRVGKD
     FDTFVAEIVK NARTGDHILV MSNGGFGGIH TKLLDALR
//
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