Bifunctional enzyme MurC/Ddl - Chlamydophila caviae

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Q821S4 (MUDD_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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/ddlA
Ordered Locus Names:	CCA_00863

Organism

Chlamydophila caviae [Complete proteome] [HAMAP]

Taxonomic identifier

83557 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	811 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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
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 – 811

811

Bifunctional enzyme MurC/Ddl HAMAP MF_00046

PRO_0000177913

Regions

Domain

574 – 785

212

ATP-grasp

Nucleotide binding

111 – 117

ATP Potential

Nucleotide binding

607 – 662

ATP By similarity

Region

1 – 450

450

UDP-N-acetylmuramate--alanine ligase HAMAP MF_00046

Region

451 – 811

361

D-alanine--D-alanine ligase HAMAP MF_00046

Sites

Metal binding

739

Magnesium or manganese 1 By similarity

Metal binding

752

Magnesium or manganese 1 By similarity

Metal binding

752

Magnesium or manganese 2 By similarity

Metal binding

754

Magnesium or manganese 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q821S4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 096AC84D620947F2
Show »

FASTA

811

90,491

        10         20         30         40         50         60 
MNRKNHYHFI GIGGIGMSAL AHILLDRGYS VSGSDLNQGI TIDKLIAKGA AYLPGHKESY 

        70         80         90        100        110        120 
VPEEGTIIYG SGIAKDNVEY KEALRKQLPL VHRAELLALL MQEQTSILVS GSHGKTTVSS 

       130        140        150        160        170        180 
LITAIFQTAK KDPSYAIGGL NSQYLNGYSG SSEYFIAEAD ESDGSLKHYF PKVAVVTNLD 

       190        200        210        220        230        240 
NEHLSNFEGS KEKLAQTIEE FTRKVDDPNL CFYNGDCQEL KGRISGISYG FSQECALYIY 

       250        260        270        280        290        300 
SHRQEGWRSV FSLSFLGKDY LDIDLNLIGK HNVANAAAAI GVALTFGIDE ESIREALKSF 

       310        320        330        340        350        360 
SGVQRRMERK NTSEKFLFLE DYAHHPSEIS CTLRALRDAV GLRRIIAICQ PHRFSRLLYC 

       370        380        390        400        410        420 
LEEFFNAFQD ADEVILTDVY SAGEMPLDLP SPEKLAETIS LSSHVCCTYV PYDNVIEHLK 

       430        440        450        460        470        480 
QNIRVHDVCI SLGAGNIHTV GNALKDFEPK KLSVGVVCGG QSCEHDVSLL SARNVVQYLS 

       490        500        510        520        530        540 
PQHYDVQYFV INRQGLWSQV ANLDAGSDYN SKNYHVLSSK IAEALANLDF VLPILHGPFG 

       550        560        570        580        590        600 
EDGTLQGFLE IANKPYGGPS LLFSAISMDK IMTKRLAASV GVPVVPYQPL TLPTWKRTPE 

       610        620        630        640        650        660 
LCMRRILETF TFPMFVKTAH LGSSIGVFEV HNETELKAKI SEAFLYDTDV FIEESRLGSR 

       670        680        690        700        710        720 
EIEVSCLGDA CSCYYISEPH ERRGSKGFIG YEEKYGFNGK SSATIQYDLN LSEESKTRVK 

       730        740        750        760        770        780 
ELTERVYRVI QGKGSCRIDF FLDREGNFWL SEMNPIPGMT KSSPFLHDFA RLGWTFEQIV 

       790        800        810 
HQLIIAGLHK FDQKKKVSST FNKQCLLTAK S

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References

[1]

"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G.

Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015925 Genomic DNA. Translation: AAP05604.1.
RefSeq	NP_829726.1. NC_003361.3.
3D structure databases
ProteinModelPortal	Q821S4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1218548.
GenomeReviews	Gene locus CCA_00863 in contig AE015925_GR.
KEGG	cca:CCA00863.
PATRIC	20270857. VBIChlCav107360_0908.
TIGR	CCA_00863.
Phylogenomic databases
HOGENOM	HBG413852.
OMA	REIEVSC.
PhylomeDB	Q821S4.
ProtClustDB	PRK14573.
Enzyme and pathway databases
BioCyc	CCAV227941:CCA_00863-MONOMER.
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. 1 hit. G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.720. 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_CHLCV

Accession

Primary (citable) accession number: Q821S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 69 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents