Bifunctional enzyme MurC/Ddl - Chlamydia trachomatis

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O84767 (MUDD_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional enzyme MurC/Ddl

Including the following 2 domains:

UDP-N-acetylmuramate--L-alanine ligase
EC=6.3.2.8
Alternative name(s):
UDP-N-acetylmuramoyl-L-alanine synthetase
D-alanine--D-alanine ligase
EC=6.3.2.4
Alternative name(s):
D-Ala-D-Ala ligase
D-alanylalanine synthetase

Gene names

Name:	murC/ddl
Ordered Locus Names:	CT_762

Organism

Chlamydia trachomatis

Taxonomic identifier

813 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
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 HAMAP MF_00046.
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 Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW D-alanine-D-alanine ligase activity Inferred from electronic annotation. Source: EC UDP-N-acetylmuramate-L-alanine ligase activity Inferred from electronic annotation. Source: EC metal 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 – 803

803

Bifunctional enzyme MurC/Ddl HAMAP MF_00046

PRO_0000177916

Regions

Domain

567 – 778

212

ATP-grasp

Nucleotide binding

111 – 117

ATP Potential

Nucleotide binding

600 – 655

ATP By similarity

Region

1 – 446

446

UDP-N-acetylmuramate--alanine ligase HAMAP MF_00046

Region

447 – 803

357

D-alanine--D-alanine ligase HAMAP MF_00046

Sites

Metal binding

732

Magnesium or manganese 1 By similarity

Metal binding

745

Magnesium or manganese 1 By similarity

Metal binding

745

Magnesium or manganese 2 By similarity

Metal binding

747

Magnesium or manganese 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O84767 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 82BB523BF1F4C1C8
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FASTA

803

89,230

        10         20         30         40         50         60 
MMKSLFYHFI GIGGIGMSAL AHVLLDRGYS VSGSDLSEGK VVEKLKNKGA EFFLGNQEEH 

        70         80         90        100        110        120 
IPEGAVVVYS SSISKKNPEF LSAKSRGNRV VHRAELLAEL AQDQISIFVT GSHGKTTVSS 

       130        140        150        160        170        180 
LITAILQEAK KNPSFAIGGL NQEGINGGSG SEYFVAEADE SDGSIRCYTP EFSVITNIDD 

       190        200        210        220        230        240 
EHLSNFEGDR ELLLASLKDF ALKTQQICWY NGDCPRLRSC LQGHTFGLDS SCDLHILSYY 

       250        260        270        280        290        300 
QEGWRLYFTA KYQDVVYADI EVQLVGMHNV LNAAAAMGIA LSLGIDEGAI RNAFRGFSGV 

       310        320        330        340        350        360 
QRRLQRKNSS ETFLFLEDYA HHPSEISCTL RAVRTAVGQR RILAIYQPHR FSRLRECIDS 

       370        380        390        400        410        420 
FPSAFKDADE VLLTEVYSAG EEAEDISYQK LAEAISQESI VKCTHIPFHE LQRHLEQSIR 

       430        440        450        460        470        480 
VHDVCVSLGA GNIVNLGEKL RDFEPQKLHL GIICGGKSCE HEISVLSAKN IAKHLSKSFY 

       490        500        510        520        530        540 
DVSYFLITRE GLWESVSSLE TAEDSGKSVF DPEIAQRLEK VDVVLPILHG PYGEDGAMQG 

       550        560        570        580        590        600 
FLETIGKPYT GPAIAFSAIA MNKVFTKRFM SDLGIPVVPY LPLTLAGWKQ EQDKWLAHIV 

       610        620        630        640        650        660 
EAFSFPIFVK SSHLGSSIGV FEVHNVIELR DAINEAFMRD NDVFVEENRL GCKEIEVSVL 

       670        680        690        700        710        720 
GDGSGAFVVA GLHERRGSGG FIDYQEKYGL SGKSSAQIVF DTDLSKEIQE QILEAADKIY 

       730        740        750        760        770        780 
RLLLGKGSCR IDFFVDEEGN FWLSEMNPIP GMTETSPFLT SFIRKGWSYE QIVHQLVIDG 

       790        800 
LQRFNQRQRL ISTSFVDQAF AIQ

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References

[1]	"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001273 Genomic DNA. Translation: AAC68357.1.
PIR	A71475.
RefSeq	NP_220281.1. NC_000117.1.
3D structure databases
ProteinModelPortal	O84767.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	884562.
GenomeReviews	Gene locus CT_762 in contig AE001273_GR.
KEGG	ctr:CT762.
PATRIC	20381212. VBIChlTra43535_0837.
Phylogenomic databases
HOGENOM	HBG413852.
OMA	REIEVSC.
ProtClustDB	PRK14573.
Family and domain databases
HAMAP	MF_00046. MurC. Fused. [Tree] MF_00047. Dala_Dala_lig. Fused. [Tree]
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. 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. IPR016040. NAD(P)-bd_dom. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR005758. UDP-N-AcMur_Ala_ligase. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
KO	K01921. K01924.
PANTHER	PTHR23135:SF5. PTHR23135:SF5. 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]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit. SSF52440. PreATP-grasp-like. 1 hit.
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_CHLTR

Accession

Primary (citable) accession number: O84767

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents