Reviewed, UniProtKB/Swiss-Prot Q9PLG1 (MUDD_CHLMU)

Names and origin

Protein names

Recommended name:
    Bifunctional enzyme murC/ddl
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylmuramate--L-alanine ligase
              EC=6.3.2.8
        Alternative name(s):
            UDP-N-acetylmuramoyl-L-alanine synthetase
    2- Recommended name:
            D-alanine--D-alanine ligase
              EC=6.3.2.4
        Alternative name(s):
            D-alanylalanine synthetase
            D-Ala-D-Ala ligase

Gene names

Name:	murC/ddl
Ordered Locus Names:	TC_0143

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cell wall formation. HAMAP MF_00046
Catalytic activity	ATP + UDP-N-acetylmuramate + L-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine. HAMAP MF_00046 ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP MF_00046
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00046
Subcellular location	Cytoplasm Probable.
Sequence similarities	In the N-terminal section; belongs to the murCDEF family. In the C-terminal section; belongs to the D-alanine--D-alanine ligase family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramate-L-alanine ligase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 802	802	Bifunctional enzyme murC/ddl HAMAP MF_00046		PRO_0000177914
Regions
	Domain	566 – 777	212	ATP-grasp
	Nucleotide binding	110 – 116	7	ATP Potential
	Nucleotide binding	599 – 654	56	ATP By similarity
	Region	1 – 445	445	UDP-N-acetylmuramate--alanine ligase HAMAP MF_00046
	Region	446 – 802	357	D-alanine--D-alanine ligase HAMAP MF_00046
Sites
	Metal binding	731	1	Magnesium or manganese 1 By similarity
	Metal binding	744	1	Magnesium or manganese 1 By similarity
	Metal binding	744	1	Magnesium or manganese 2 By similarity
	Metal binding	746	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PLG1-1 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 3FAF071C3CB78F96	FASTA	802	88,744
	10 20 30 40 50 60 MKSLCYHFIG IGGIGMSALA HILLDRGYSV SGSDLSEGKI VETLKNKGVK FFLGNQEEHV 70 80 90 100 110 120 PEESVVVYGS GISKNNPEFL AALNKGNRLI HRAELLAELT KEQISIFVTG SHGKTTVSSL 130 140 150 160 170 180 ITVILQEAGK TPSFAIGGLN GEGINGSSGS EYFVAEADES DGSIRNYSPE FSVITNIDDE 190 200 210 220 230 240 HLSNFGGDRE RLLASLQDFS TKTRQICWYN GDCSRLRSCL VGHTFGFTSS CDLHILTYRQ 250 260 270 280 290 300 EGWRSFFTVR YQNVLYEDVE VRLVGEHNVM NAAAAMGVAL SLGIDEDTIR DALQRFPGVQ 310 320 330 340 350 360 RRLQRKNSSE VFLFLEDYAH HPSEIACTLQ AVRSAVGSRR VLAICQPHRF SRLKECMGCF 370 380 390 400 410 420 PSAFKGADEV LLTDVYSAGE AEEDVSYKEL AQSISRESLV TCAYVPFSEL QGFLEKHIRV 430 440 450 460 470 480 HDVCVALGAG DIEVLGESLR DFEPKKLSLG LICGGRSCEH DISILSAQNI AKYLSHSFYE 490 500 510 520 530 540 VQYFLITREG LWKTGSSLEL SEETGKTIFD PEIAGKLSKV DVILPILHGP YGEDGAMQGF 550 560 570 580 590 600 LETIGKPYTG PSLVFAAIGM NKVLTKRFMS DLGIPVVPYL PLTLKGWKQD QEKCLAQIKA 610 620 630 640 650 660 AFSFPMFVKS VHLGSSIGVF EVHDTNELRD AINEAFVRDD DVFIEESRLG CREIEVSFLG 670 680 690 700 710 720 DGSGVFFVAG MHERRGRGGF IDYQEKYGLS GRASAQIVFD VDLSKETREQ LLGVAEKIYR 730 740 750 760 770 780 LLQGKGSCRI DFFVDNEGSF WLSEINPIPG MTTASPFLAA FVRKGWNREQ IVHQLVIDGL 790 800 QRFDQRQRLI STPLIDQALA AR

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE002160 Genomic DNA. Translation: AAF39021.1. Different initiation.
PIR	B81737.
RefSeq	NP_296522.1.
3D structure databases
HSSP	HSSP built from PDB template 1GQY based on UniProtKB P45066.
ModBase	Search...
Genome annotation databases
GeneID	1245677.
GenomeReviews	Gene locus TC_0143 in contig AE002160_GR.
KEGG	cmu:TC0143.
TIGR	TC_0143.
Phylogenomic databases
HOGENOM	Q9PLG1.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0143-MON.
BRENDA	6.3.2.4. 256349. 6.3.2.8. 256349.
Family and domain databases
HAMAP	MF_00046. Fused. [Tree] MF_00047. Fused. [Tree]
InterPro	IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR000291. D-Ala_lig_Van_CS. IPR005905. D_ala_D_ala. IPR011095. Dala_Dala_lig_C. IPR011127. Dala_Dala_lig_N. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR013817. Pre-ATP_grasp. IPR005758. UDP-N-AcMur_Ala_ligase. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 1 hit. PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01205. D_ala_D_alaTIGR. 1 hit. TIGR01082. murC. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00843. DALA_DALA_LIGASE_1. 1 hit. PS00844. DALA_DALA_LIGASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MUDD_CHLMU

Accession

Primary (citable) accession number: Q9PLG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)