(data stored in SCRATCH zone)

SWISSPROT: A1AZK5_PARDP

ID   A1AZK5_PARDP            Unreviewed;       461 AA.
AC   A1AZK5;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 96.
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   OrderedLocusNames=Pden_0587 {ECO:0000313|EMBL:ABL68699.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68699.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
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.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final
CC       step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the
CC       precursor of 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-
CC         L-alanyl-gamma-D-glutamyl-L-lysine = ADP + H(+) + phosphate +
CC         UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-
CC         D-alanyl-D-alanine; Xref=Rhea:RHEA:16085, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57822,
CC         ChEBI:CHEBI:70758, ChEBI:CHEBI:83903, ChEBI:CHEBI:456216;
CC         EC=6.3.2.10; Evidence={ECO:0000256|HAMAP-Rule:MF_02019,
CC         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; CP000489; ABL68699.1; -; Genomic_DNA.
DR   RefSeq; WP_011746932.1; NC_008686.1.
DR   STRING; 318586.Pden_0587; -.
DR   PRIDE; A1AZK5; -.
DR   EnsemblBacteria; ABL68699; ABL68699; Pden_0587.
DR   KEGG; pde:Pden_0587; -.
DR   eggNOG; ENOG4107EES; Bacteria.
DR   eggNOG; COG0770; LUCA.
DR   HOGENOM; HOG000268120; -.
DR   KO; K01929; -.
DR   OMA; SYNNHWG; -.
DR   BioCyc; PDEN318586:G1GW1-595-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000361; Chromosome 1.
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: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_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   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; TIGR01143; murF; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZK5.
DR   SWISS-2DPAGE; A1AZK5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:ABL68699.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02019,
KW   ECO:0000256|RuleBase:RU004136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN       24     93       Mur_ligase. {ECO:0000259|Pfam:PF01225}.
FT   DOMAIN      106    292       Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
FT   DOMAIN      323    376       Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
FT   NP_BIND     108    114       ATP. {ECO:0000256|HAMAP-Rule:MF_02019}.
SQ   SEQUENCE   461 AA;  47944 MW;  16BA0C34958C84D5 CRC64;
     MTLWTSQDAA EATGGRATRD FAVGGVSIDT RTIRPGDLFV ALQAARDGHD FVARALEKGA
     CAALVSRIPE GVAPDAPLLV VPDVLPALEA LGRAGRARMR GKVVAITGSV GKTSTKEMAR
     VALAGQGRVH AAEASYNNHW GVPLTLARMP EDTDFAIVEI GMNHPGEIEP LARLARPHVA
     MVTTVAAAHL EAFGAIEGIA REKGAIFRGL IQPGTAIIPE DLPVTQLLRD CADDAAAIVI
     GFGQQGMARP LKAETLDGVT RVRARVLGET VDFMLASAGT HFVMNAVGML AALSAAGADV
     AEAAKHLSDW RPPLGRGAVE DLDGIRLIDD AYNSNPTSLS AGLATLARLT GGRRVAILGD
     MLELGPDEIA LHAGMAGDPA MEAVDLVHTA GPRMRALHEA LPQGRRGMHA ETAAELAGKV
     GELVASGDIV LVKGSKSSKV STVVDALRRT RQSTPPGERT A
//

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