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Database: UniProt
Entry: Q12RI0_SHEDO
LinkDB: Q12RI0_SHEDO
Original site: Q12RI0_SHEDO 
ID   Q12RI0_SHEDO            Unreviewed;       464 AA.
AC   Q12RI0;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
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   OrderedLocusNames=Sden_0656 {ECO:0000313|EMBL:ABE53946.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE53946.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE53946.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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; CP000302; ABE53946.1; -; Genomic_DNA.
DR   RefSeq; WP_011495111.1; NC_007954.1.
DR   AlphaFoldDB; Q12RI0; -.
DR   STRING; 318161.Sden_0656; -.
DR   KEGG; sdn:Sden_0656; -.
DR   eggNOG; COG0773; Bacteria.
DR   HOGENOM; CLU_028104_0_1_6; -.
DR   OMA; SGIAWDH; -.
DR   OrthoDB; 9804126at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001982; 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:UP000001982}.
FT   DOMAIN          2..103
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          112..304
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          325..372
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         114..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02020"
SQ   SEQUENCE   464 AA;  50462 MW;  ED19C54B3791C86C CRC64;
     MHVHILGICG TFMGGLALLA RAMGHKVTGS DANVYPPMST QLLEQGIELI QGFDPSQLGD
     SDENAPDLVV IGNAMSRGNP CVEAVLNRGL KYTSGPQFLA EHILPGRWVL AVSGTHGKTS
     TSSMLAWILE YSGYEPGFLI GGVPQNFGVS ARLGNSNFFV VEADEYDSAF FDKRSKFVHY
     QPRTLVINNL EFDHADIFDD LTAIQRQFNH VIRTVPGQGK IIWPANSEAV QQVIEMGCWS
     EQETYSAGVH DFNTEKTLGW HAKTLSADAH EFEVYFDGHS QGVMSWNLIG QHNVENAVMA
     IAAARHVGVV PAQAMAALSE FSPPKRRLEL LGTIGGVAVF DDFAHHPTAI DSTLQGLRAK
     VGNGKITVVL EPRSNTMKQG VHKDTLAHSL VRADQAYLYQ ADSISWDLKS SMQTASIPVS
     VKTDIEQIID ALCHDAKAGD TIVIMSNGGF NGIHKKLLEA LADR
//
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