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Protein

Capsule biosynthesis protein CapD

Gene

capD

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transpeptidase that cleaves the poly-gamma-D-glutamate capsule and catalyzes the formation of an amide bond with the side-chain amino group of meso-diaminopimelic acid (m-DAP) in the peptidoglycan scaffold (PubMed:19017271). Degradation of the high-molecular weight capsule (H-capsule) to the lower-molecular weight capsule (L-capsule), which is released from the bacterial cell surface. The production of L-capsule is essential to mediate escape from host defenses.4 Publications

Pathwayi: capsule polysaccharide biosynthesis

This protein is involved in the pathway capsule polysaccharide biosynthesis, which is part of Capsule biogenesis.
View all proteins of this organism that are known to be involved in the pathway capsule polysaccharide biosynthesis and in Capsule biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131GlutamateBy similarity
Active sitei352 – 3521Nucleophile2 Publications
Binding sitei370 – 3701GlutamateBy similarity
Binding sitei389 – 3891GlutamateBy similarity
Binding sitei520 – 5201GlutamateCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Transferase

Keywords - Biological processi

Capsule biogenesis/degradation, Virulence

Enzyme and pathway databases

BioCyciANTHRA:GBAA_PXO2_0063-MONOMER.
BANT261594:GJ7F-5855-MONOMER.
UniPathwayiUPA00934.

Protein family/group databases

MEROPSiT03.023.

Names & Taxonomyi

Protein namesi
Recommended name:
Capsule biosynthesis protein CapD (EC:2.3.2.-)
Cleaved into the following 2 chains:
Gene namesi
Name:capD
Synonyms:dep
Ordered Locus Names:pXO2-55, BXB0063, GBAA_pXO2_0063
Encoded oniPlasmid pXO24 Publications
Plasmid pTE7021 Publication
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Plasmid pXO2

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi368 – 3681T → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi370 – 3701T → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi372 – 3721S → A: Slightly reduces enzyme activity. 1 Publication
Mutagenesisi520 – 5201R → A: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 528502Capsule biosynthesis protein CapD large chainPRO_0000205980Add
BLAST
Chaini352 – 528177Capsule biosynthesis protein CapD small chainPRO_0000424555Add
BLAST

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.

Keywords - PTMi

Zymogen

Expressioni

Inductioni

Capsule synthesis is transcriptionally regulated by AtxA, AcpA and AcpB.1 Publication

Interactioni

Subunit structurei

This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.1 Publication

Structurei

Secondary structure

1
528
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 556Combined sources
Helixi56 – 6712Combined sources
Helixi72 – 8615Combined sources
Turni87 – 904Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi107 – 1115Combined sources
Helixi132 – 14312Combined sources
Helixi148 – 16114Combined sources
Helixi167 – 18014Combined sources
Helixi183 – 1853Combined sources
Helixi186 – 1883Combined sources
Helixi190 – 1923Combined sources
Helixi204 – 21613Combined sources
Helixi219 – 2224Combined sources
Helixi224 – 23411Combined sources
Helixi238 – 2425Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi259 – 2635Combined sources
Helixi270 – 28213Combined sources
Helixi285 – 2884Combined sources
Helixi292 – 31221Combined sources
Helixi324 – 3274Combined sources
Helixi330 – 3345Combined sources
Beta strandi353 – 3586Combined sources
Beta strandi364 – 3707Combined sources
Turni374 – 3774Combined sources
Beta strandi414 – 4185Combined sources
Beta strandi421 – 4266Combined sources
Helixi430 – 4323Combined sources
Helixi433 – 44513Combined sources
Helixi451 – 4566Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi466 – 4716Combined sources
Helixi475 – 4828Combined sources
Turni483 – 4853Combined sources
Beta strandi487 – 4904Combined sources
Helixi494 – 4974Combined sources
Beta strandi501 – 5066Combined sources
Turni507 – 5104Combined sources
Beta strandi511 – 5155Combined sources
Helixi518 – 5203Combined sources
Beta strandi523 – 5264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G9KX-ray1.79D/L29-351[»]
F/S352-528[»]
3GA9X-ray2.30L29-351[»]
S352-528[»]
ProteinModelPortaliQ51693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51693.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni429 – 4324Glutamate bindingCombined sources1 Publication

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000175617.
KOiK00681.
OMAiKPFMVIG.
OrthoDBiEOG62K1RV.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q51693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSFKWGKKI ILFCLIVSLM GGIGVSCSFN KIKDSVKQKI DSMGDKGTYG
60 70 80 90 100
VSASHPLAVE EGMKVLKNGG SAVDAAIVVS YVLGVVELHA SGIGGGGGML
110 120 130 140 150
IISKDKETFI DYRETTPYFT GNQKPHIGVP GFVAGMEYIH DNYGSLPMGE
160 170 180 190 200
LLQPAINYAE KGFKVDDSLT MRLDLAKPRI YSDKLSIFYP NGEPIETGET
210 220 230 240 250
LIQTDLARTL KKIQKEGAKG FYEGGVARAI SKTAKISLED IKGYKVEVRK
260 270 280 290 300
PVKGNYMGYD VYTAPPPFSG VTLLQMLKLA EKKEVYKDVD HTATYMSKME
310 320 330 340 350
EISRIAYQDR KKNLGDPNYV NMDPNKMVSD KYISTMKNEN GDALSEAEHE
360 370 380 390 400
STTHFVIIDR DGTVVSSTNT LSNFFGTGKY TAGFFLNNQL QNFGSEGFNS
410 420 430 440 450
YEPGKRSRTF MAPTVLKKDG ETIGIGSPGG NRIPQILTPI LDKYTHGKGS
460 470 480 490 500
LQDIINEYRF TFEKNTAYTE IQLSSEVKNE LSRKGLNVKK KVSPAFFGGV
510 520
QALIKDERDN VITGAGDGRR NGTWKSNK
Length:528
Mass (Da):58,084
Last modified:September 27, 2004 - v2
Checksum:i5CC4CF263D650BF3
GO

Sequence cautioni

The sequence AAF13660.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA03126.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti400 – 4001S → N in strain: Pasteur.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14037 Genomic DNA. Translation: BAA03126.1. Different initiation.
AF188935 Genomic DNA. Translation: AAF13660.1. Different initiation.
AE011191 Genomic DNA. Translation: AAM26219.1.
AE017335 Genomic DNA. Translation: AAT28993.2.
PIRiS36209.
RefSeqiNP_053210.1. NC_002146.1.
WP_010891443.1. NC_002146.1.

Genome annotation databases

EnsemblBacteriaiAAM26219; AAM26219; BX_B0063.
AAT28993; AAT28993; GBAA_pXO2_0063.
GeneIDi3361854.
KEGGibanh:HYU01_29295.
bar:GBAA_pXO2_0063.
pg:3361854.
PATRICi24662354. VBIBacAnt106580_0266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14037 Genomic DNA. Translation: BAA03126.1. Different initiation.
AF188935 Genomic DNA. Translation: AAF13660.1. Different initiation.
AE011191 Genomic DNA. Translation: AAM26219.1.
AE017335 Genomic DNA. Translation: AAT28993.2.
PIRiS36209.
RefSeqiNP_053210.1. NC_002146.1.
WP_010891443.1. NC_002146.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G9KX-ray1.79D/L29-351[»]
F/S352-528[»]
3GA9X-ray2.30L29-351[»]
S352-528[»]
ProteinModelPortaliQ51693.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiT03.023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM26219; AAM26219; BX_B0063.
AAT28993; AAT28993; GBAA_pXO2_0063.
GeneIDi3361854.
KEGGibanh:HYU01_29295.
bar:GBAA_pXO2_0063.
pg:3361854.
PATRICi24662354. VBIBacAnt106580_0266.

Phylogenomic databases

HOGENOMiHOG000175617.
KOiK00681.
OMAiKPFMVIG.
OrthoDBiEOG62K1RV.

Enzyme and pathway databases

UniPathwayiUPA00934.
BioCyciANTHRA:GBAA_PXO2_0063-MONOMER.
BANT261594:GJ7F-5855-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ51693.
PROiQ51693.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis."
    Uchida I., Makino S., Sasakawa C., Yoshikawa M., Sugimoto C., Terakado N.
    Mol. Microbiol. 9:487-496(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: Davis.
    Plasmid: pTE702
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Pasteur.
    Plasmid: pXO2
  3. "Comparative genome sequencing for discovery of novel polymorphisms in Bacillus anthracis."
    Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L., Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P., Fraser C.M.
    Science 296:2028-2033(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Ames / isolate Florida / A2012.
    Plasmid: pXO2
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
    Plasmid: pXO2
  5. "Effect of the lower molecular capsule released from the cell surface of Bacillus anthracis on the pathogenesis of anthrax."
    Makino S., Watarai M., Cheun H.-I., Shirahata T., Uchida I.
    J. Infect. Dis. 186:227-233(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "atxA controls Bacillus anthracis capsule synthesis via acpA and a newly discovered regulator, acpB."
    Drysdale M., Bourgogne A., Hilsenbeck S.G., Koehler T.M.
    J. Bacteriol. 186:307-315(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Plasmid: pXO2
  7. "Capsule anchoring in Bacillus anthracis occurs by a transpeptidation reaction that is inhibited by capsidin."
    Richter S., Anderson V.J., Garufi G., Lu L., Budzik J.M., Joachimiak A., He C., Schneewind O., Missiakas D.
    Mol. Microbiol. 71:404-420(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE.
  8. "Crystal structure of Bacillus anthracis transpeptidase enzyme CapD."
    Wu R., Richter S., Zhang R.G., Anderson V.J., Missiakas D., Joachimiak A.
    J. Biol. Chem. 284:24406-24414(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 29-528 IN COMPLEX WITH GLUTAMYLGLUTAMATE, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF THR-368; THR-370; SER-372 AND ARG-520, AUTOCATALYTIC CLEAVAGE.

Entry informationi

Entry nameiCAPD_BACAN
AccessioniPrimary (citable) accession number: Q51693
Secondary accession number(s): Q6F034, Q8KYD9, Q9RMX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: May 11, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.