(data stored in SCRATCH zone)

SWISSPROT: A5GRL8_SYNR3

ID   A5GRL8_SYNR3            Unreviewed;       494 AA.
AC   A5GRL8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000256|HAMAP-Rule:MF_00208,
GN   ECO:0000313|EMBL:CAK27527.1};
GN   OrderedLocusNames=SynRCC307_0624 {ECO:0000313|EMBL:CAK27527.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27527.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27527.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC       (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + meso-2,6-diaminopimelate + UDP-N-acetyl-alpha-D-
CC         muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-
CC         acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-
CC         diaminopimelate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791,
CC         ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216;
CC         EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135,
CC       ECO:0000256|SAAS:SAAS00951514}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
CC       ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}.
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000256|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
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DR   EMBL; CT978603; CAK27527.1; -; Genomic_DNA.
DR   RefSeq; WP_011935042.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0624; -.
DR   EnsemblBacteria; CAK27527; CAK27527; SynRCC307_0624.
DR   KEGG; syr:SynRCC307_0624; -.
DR   eggNOG; ENOG4107EEN; Bacteria.
DR   eggNOG; COG0769; LUCA.
DR   HOGENOM; HOG000268118; -.
DR   KO; K01928; -.
DR   OMA; CFMEVSS; -.
DR   OrthoDB; 1861122at2; -.
DR   BioCyc; SSP316278:G1GJL-618-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; 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-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_00208; MurE; 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; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
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   SUPFAM; SSF63418; SSF63418; 1.
DR   TIGRFAMs; TIGR01085; murE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRL8.
DR   SWISS-2DPAGE; A5GRL8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951530};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951553};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951545};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951519};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:CAK27527.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|SAAS:SAAS00951542};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
KW   ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   DOMAIN       32    106       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      118    318       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      339    425       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     120    126       ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      162    163       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   REGION      415    418       Meso-diaminopimelate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   MOTIF       415    418       Meso-diaminopimelate recognition motif.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING      35     35       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     189    189       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     195    195       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     197    197       UDP-MurNAc-L-Ala-D-Glu.
FT                                {ECO:0000256|HAMAP-Rule:MF_00208}.
FT   BINDING     391    391       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   BINDING     466    466       Meso-diaminopimelate; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00208}.
FT   BINDING     470    470       Meso-diaminopimelate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
FT   MOD_RES     229    229       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_00208}.
SQ   SEQUENCE   494 AA;  51946 MW;  C7C00FBDA119AEDC CRC64;
     MASEASRLHL LIRDAGLSVP QQLPDPVVTD FSCDSRRIRP GTLFVGLPGG RVDGGSFWRA
     ALQQGATAAV IGPDAAQQEP PAPGDPVLVV ADPVAAAAGR LAAAFWNHPS DQLSLIGVTG
     TNGKTTTTHL IEHLALACGS PTALMGTLAN RWPGHSRNAV HTTPFADQLQ ADLAAAKAAG
     CSMAAMEVSS HALDQSRVAG CRFSGAVFTN LSQDHLDYHP TLEDYFEAKA QLFAAPYLKG
     QAVVNSDDLH GRQLAQRLGD QCWRSSLEDS SAELFMDGLQ FSATGVKGVL HGPSGDVPFQ
     SPLVGRFNLM NLLQAVGVLL QHGLPCDGLL QALESFNGVP GRMERVPHRS DQPAVLVDYA
     HTPDGLDNAL QAARPFAEGK LICVFGCGGD RDRSKRPQMG AIAAQLADEL VVTSDNPRTE
     DPQQILDDVV AGIPAESACV VVADRAAAIA QAIGQAKAGD LVLIAGKGHE DYQILGTTKV
     HFDDREEAAK ALQG
//

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