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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)DescriptionActionsGraphical viewLength
Binding sitei113GlutamateBy similarity1
Active sitei352Nucleophile2 Publications1
Binding sitei370GlutamateBy similarity1
Binding sitei389GlutamateBy similarity1
Binding sitei520GlutamateCombined sources1 Publication1

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.
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)DescriptionActionsGraphical viewLength
Mutagenesisi368T → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi370T → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi372S → A: Slightly reduces enzyme activity. 1 Publication1
Mutagenesisi520R → A: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000020598027 – 528Capsule biosynthesis protein CapD large chainAdd BLAST502
ChainiPRO_0000424555352 – 528Capsule biosynthesis protein CapD small chainAdd BLAST177

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

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 55Combined sources6
Helixi56 – 67Combined sources12
Helixi72 – 86Combined sources15
Turni87 – 90Combined sources4
Beta strandi95 – 102Combined sources8
Beta strandi107 – 111Combined sources5
Helixi132 – 143Combined sources12
Helixi148 – 161Combined sources14
Helixi167 – 180Combined sources14
Helixi183 – 185Combined sources3
Helixi186 – 188Combined sources3
Helixi190 – 192Combined sources3
Helixi204 – 216Combined sources13
Helixi219 – 222Combined sources4
Helixi224 – 234Combined sources11
Helixi238 – 242Combined sources5
Beta strandi247 – 249Combined sources3
Beta strandi252 – 256Combined sources5
Beta strandi259 – 263Combined sources5
Helixi270 – 282Combined sources13
Helixi285 – 288Combined sources4
Helixi292 – 312Combined sources21
Helixi324 – 327Combined sources4
Helixi330 – 334Combined sources5
Beta strandi353 – 358Combined sources6
Beta strandi364 – 370Combined sources7
Turni374 – 377Combined sources4
Beta strandi414 – 418Combined sources5
Beta strandi421 – 426Combined sources6
Helixi430 – 432Combined sources3
Helixi433 – 445Combined sources13
Helixi451 – 456Combined sources6
Beta strandi460 – 463Combined sources4
Beta strandi466 – 471Combined sources6
Helixi475 – 482Combined sources8
Turni483 – 485Combined sources3
Beta strandi487 – 490Combined sources4
Helixi494 – 497Combined sources4
Beta strandi501 – 506Combined sources6
Turni507 – 510Combined sources4
Beta strandi511 – 515Combined sources5
Helixi518 – 520Combined sources3
Beta strandi523 – 526Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G9KX-ray1.79D/L29-351[»]
F/S352-528[»]
3GA9X-ray2.30L29-351[»]
S352-528[»]
ProteinModelPortaliQ51693.
SMRiQ51693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51693.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni429 – 432Glutamate bindingCombined sources1 Publication4

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000175617.
KOiK00681.
OMAiKPFMVIG.

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti400S → N in strain: Pasteur. 1

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G9KX-ray1.79D/L29-351[»]
F/S352-528[»]
3GA9X-ray2.30L29-351[»]
S352-528[»]
ProteinModelPortaliQ51693.
SMRiQ51693.
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.
PATRICi24662354. VBIBacAnt106580_0266.

Phylogenomic databases

HOGENOMiHOG000175617.
KOiK00681.
OMAiKPFMVIG.

Enzyme and pathway databases

UniPathwayiUPA00934.
BioCyciANTHRA:GBAA_PXO2_0063-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...

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: November 30, 2016
This is version 101 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.