(data stored in SCRATCH zone)

SWISSPROT: D3VIK7_XENNA

ID   D3VIK7_XENNA            Unreviewed;       456 AA.
AC   D3VIK7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 50.
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   ECO:0000313|EMBL:CBJ88557.1};
GN   OrderedLocusNames=XNC1_0483 {ECO:0000313|EMBL:CBJ88557.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88557.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88557.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D-
CC       glutamyl-meso-diaminopimelate by linking it to UDP-N-
CC       acetylmuramate. {ECO:0000256|HAMAP-Rule:MF_02020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanyl-gamma-D-glutamyl-meso-diaminopimelate +
CC         UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-
CC         diaminopimelate; 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; Evidence={ECO:0000256|HAMAP-
CC         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; FN667742; CBJ88557.1; -; Genomic_DNA.
DR   RefSeq; WP_010845226.1; NC_014228.1.
DR   STRING; 406817.XNC1_0483; -.
DR   EnsemblBacteria; CBJ88557; CBJ88557; XNC1_0483.
DR   KEGG; xne:XNC1_0483; -.
DR   eggNOG; ENOG4105DFU; Bacteria.
DR   eggNOG; COG0773; LUCA.
DR   HOGENOM; HOG000256032; -.
DR   KO; K02558; -.
DR   OMA; CDANVYP; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 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   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01081; mpl; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIK7.
DR   SWISS-2DPAGE; D3VIK7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02020, ECO:0000313|EMBL:CBJ88557.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN        2     98       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      108    291       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      312    360       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     110    116       ATP. {ECO:0000256|HAMAP-Rule:MF_02020}.
SQ   SEQUENCE   456 AA;  49894 MW;  7128A45014FDA24D CRC64;
     MRIHLLGICG TFMGGLAILA RSLGHEVTGS DASVYPPMST LLEKQGIELI QGYDPAQLDP
     VPDIVIIGNA MTRGNPCVEA VLDRGIPYTS GPQWLHDHVL PERWVLAVAG THGKTTTAGM
     LAWVLEACGY KPGFLIGGVP GNFAVSAQIG ESPFFVIEAD EYDSAFFDKR SKFVHYSPRT
     LIMNNLEFDH ADIFENLASI QKQFHHLVRV VPSTGKIIVP DNDINLKHVL SMGCWSEQEQ
     LGDGGSWQAK KLSQDSSNYQ VFHHGEWVGE VNWSLVGEHN MHNGLMAIAA AHHIGIQPAD
     ACQALGEFIN ARRRLELRGE VNGISVYDDF AHHPTAILAT LEALRSKVGG VARILAVLEP
     RSNTMKMGMS KSDIAPSMGR ADEVFLYQPV NMPWQVVEIA EQCVQPARWS ADIDTLVRMI
     VETAQPGDHI LVMSNGGFDG IHEKLLTELA KKADAV
//

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