NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SSI-1 / Serotype M3;
DOI=10.1101/gr.1096703; PubMed=12799345 [NCBI, ExPASy, EBI, Israel, Japan]
Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y., Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H., Hattori M., Hamada S.;
"Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution.";
Genome Res. 13:1042-1055(2003).

Comments

FUNCTION: Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan (By similarity).
CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine.
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
PTM: Carbamoylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP (By similarity).
SIMILARITY: Belongs to the murCDEF family. MurE subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE014074; AAM78891.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000034; BAC64670.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_664088.1; -.
NP_802837.1; -.

3D structure databases

HSSP

P22188; 1E8C. [HSSP ENTRY / PDB]

ModBase

Q8K8H6.

Enzyme and pathway databases

BioCyc

SPYO193567:SPS1575-MON; -.
SPYO198466:SPYM3_0284-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0047482;	Molecular function: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity (inferred from electronic annotation from EC).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from InterPro).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00208; -; 1.
PBIL [Tree]

InterPro

IPR004101; Mur_ligase_C.
IPR013221; Mur_ligase_cen.
IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.190.20; Mur_ligase_C; 1.
G3DSA:3.40.1190.10; Mur_ligase_cen; 1.

Pfam

PF02875; Mur_ligase_C; 1.
PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01085; murE; 1.

ProtoNet

Q8K8H6.

Genome annotation databases

GeneID

1008598; -.
1065187; -.

GenomeReviews

BA000034_GR; SPs1575.
AE014074_GR; SpyM3_0284.

KEGG

spg:SpyM3_0284; -.
sps:SPs1575; -.

Phylogenomic databases

HOGENOM

Q8K8H6; -.

Genome annotation databases

CMR

Q8K8H6; SpyM3_0284.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Peptidoglycan synthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 481`	`481`	`UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase.`	`PRO_0000101956`
`NP_BIND`	`118 124`	`7`	`ATP (Potential).`
`REGION`	`160 161`	`2`	`UDP-MurNAc-L-Ala-D-Glu binding (By similarity).`
`MOTIF`	`404 407`	`4`	`L-lysine recognition motif.`
`BINDING`	`42 42`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`BINDING`	`158 158`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`BINDING`	`187 187`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`BINDING`	`195 195`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`MOD_RES`	`229 229`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 481 AA [This is the length of the unprocessed precursor]

Molecular weight: 53627 Da [This is the MW of the unprocessed precursor]

CRC64: DE68EAFB114CF39F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MITIEQLLDI LKKDHNFREV LDADEYHYHY QGFSFERLSY DSRQVDGKTL FFAKGATFKA 

        70         80         90        100        110        120 
DYLKEAITNG LQLYISEVDY ELGIPVVLVT DIKKAMSLIA MAFYGNPQEK LKLLAFTGTK 

       130        140        150        160        170        180 
GKTTAAYFAY HMLKESYKPA MFSTMNTTLD GKTFFKSQLT TPESLDLFAM MAECVTNGMT 

       190        200        210        220        230        240 
HLIMEVSSQA YLVDRVYGLT FDVGVFLNIS PDHIGPIEHP TFEDYFYHKR LLMENSRAVV 

       250        260        270        280        290        300 
INSVMDHFSF LADQVADQEH VFYGPLSDNQ ITTSQAFSFE AKGQLAGHYD IQLIGHFNQE 

       310        320        330        340        350        360 
NAMAAGLACL RLGASLADIQ KGIAKTRVPG RMEVLTMTNH AKVFVDYAHN GDSLEKLLSV 

       370        380        390        400        410        420 
VEEHQTGKLM LILGAPGNKG ESRRADFGRV IHQHPNLTVI LTADDPNFED PEDISKEIAS 

       430        440        450        460        470        480 
HIARPVEIIS DREQAIQKAM SLCQGAKDAV IIAGKGADAY QIVKGQQVAY AGDLAIAKHY 


L

Q8K8H6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools