GenomeNet

Database: UniProt/TrEMBL
Entry: W6EEV5_SULMU
LinkDB: W6EEV5_SULMU
Original site: W6EEV5_SULMU 
 KJW12223; KJW12223; VC81_10035.
DR   PATRIC; fig|216463.3.peg.1265; -.
DR   Proteomes; UP000033491; Unassembled WGS sequence.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000033491};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    131       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002465848.
SQ   SEQUENCE   131 AA;  15308 MW;  46A687D6FDD73A2C CRC64;
     MFKKIIQTSL VSLALVGGIT ITVQPQTAHA KKLTTSLIHR HYMAEYRIKV KKNMPMYKQR
     LDNEGRIRGY KKVTLHKGEI VRTWYRQVGG VSWQVTGGKY SKSKHYQYSV NFTNTRQFKI
     LHTYPASKGW F
//
ID   A0A0F3RQP2_9LACO        Unreviewed;       459 AA.
AC   A0A0F3RQP2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   20-JUN-2018, entry version 21.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382177};
DE            EC=6.3.2.9 {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382044};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000256|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000256|HAMAP-Rule:MF_00639,
GN   ECO:0000313|EMBL:KJW12296.1};
GN   ORFNames=VC81_10435 {ECO:0000313|EMBL:KJW12296.1};
OS   Lactobacillus spicheri.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW12296.1, ECO:0000313|Proteomes:UP000033491};
RN   [1] {ECO:0000313|EMBL:KJW12296.1, ECO:0000313|Proteomes:UP000033491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP38 {ECO:0000313|EMBL:KJW12296.1,
RC   ECO:0000313|Proteomes:UP000033491};
RA   Zheng J., Ganezle M.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS00382010}.
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
CC       + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC       alanyl-D-glutamate. {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00382107}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00639, ECO:0000256|RuleBase:RU003664,
CC       ECO:0000256|SAAS:SAAS00382165}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
CC       ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084461}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00639, ECO:0000256|SAAS:SAAS00569906}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJW12296.1}.
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DR   EMBL; JZCR01000021; KJW12296.1; -; Genomic_DNA.
DR   RefSeq; WP_045808020.1; NZ_JZCR01000021.1.
DR   EnsemblBacteria; KJW12296; KJW12296; VC81_10435.
DR   PATRIC; fig|216463.3.peg.1345; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000033491; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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_00639; MurD; 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; IPR005762; UDP-N-AcMur-Glu_ligase.
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; TIGR01087; murD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084371};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459080};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084380};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00084500};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|RuleBase:RU003664, ECO:0000256|SAAS:SAAS00459111};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033491};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084399};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00639,
KW   ECO:0000256|SAAS:SAAS00084447, ECO:0000313|EMBL:KJW12296.1};
KW   Nucleotide-bi
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