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Protein

Carboxy-terminal processing protease CtpB

Gene

ctpB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.4 Publications

Catalytic activityi

The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.1 Publication

Enzyme regulationi

Activated by peptide binding to the PDZ domain.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei168 – 1681Crucial for substrate binding and protease activation1 Publication
Active sitei309 – 3091Nucleophile1 Publication
Active sitei334 – 3341Charge relay system1 Publication
Active sitei338 – 3381Charge relay system1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • peptidase activity Source: UniProtKB
  • peptide binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • serine-type peptidase activity Source: UniProtKB-KW

GO - Biological processi

  • peptide metabolic process Source: UniProtKB
  • proteolysis Source: UniProtKB
  • signal transduction Source: UniProtKB
  • sporulation resulting in formation of a cellular spore Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU35240-MONOMER.

Protein family/group databases

MEROPSiS41.007.
TCDBi9.B.174.1.1. the two tunnel gated c-terminal processing protease (ctp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxy-terminal processing protease CtpB (EC:3.4.21.1021 Publication)
Short name:
C-terminal processing protease
Gene namesi
Name:ctpB
Synonyms:yvjB
Ordered Locus Names:BSU35240
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Forespore intermembrane space 1 Publication

  • Note: Is expressed in both the mother cell and forespore compartments but that synthesis in the forespore is both necessary and sufficient for the proper timing of pro-sigma-K processing.

Pathology & Biotechi

Disruption phenotypei

Pro-sigma-K processing is delayed by approximately 30 minutes, and sporulation efficiency is reduced approximately two-fold.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 405AAVPA → RAVPR: No cleavage by SpoIVB. No effect on pro-sigma-K processing. 1 Publication
Mutagenesisi92 – 18291Missing : Constitutively active protease with higher activity than wild-type protease and total loss of substrate specificity. 1 PublicationAdd
BLAST
Mutagenesisi118 – 1181V → Y: Loss of peptide binding to the PDZ domain, but still has residual protease activity. Less than residual protease activity; when associated with A/F-168. 1 Publication
Mutagenesisi168 – 1681R → A or F: 3- to 5-fold weaker affinity for PDZ ligands and reduced proteolytic activity against pre-processed SpoIVFA substrate. Less than residual protease activity; when associated with Y-118. 1 Publication
Mutagenesisi309 – 3091S → A: Loss of activity. 1 Publication
Mutagenesisi338 – 3381Q → E: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 480457Carboxy-terminal processing protease CtpBPRO_0000390777Add
BLAST

Post-translational modificationi

Is cleaved by SpoIVB in vitro and in vivo but this cleavage does not appear to be necessary for CtpB activation. CtpB can also cleave itself in vivo.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei36 – 372Cleavage; by SpoIVB, and cleavage; by autolysis1 Publication
Sitei40 – 412Cleavage; by SpoIVB
Sitei42 – 432Cleavage; by autolysis1 Publication

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiO35002.

Expressioni

Developmental stagei

Is expressed in the forespore under the control of sigma-G, and in the mother cell under the control of sigma-E.2 Publications

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-5246793,EBI-5246793
spoIVFAP269362EBI-5246793,EBI-5254757

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

IntActiO35002. 3 interactions.
STRINGi224308.Bsubs1_010100019066.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 6520Combined sources
Beta strandi66 – 683Combined sources
Helixi72 – 8514Combined sources
Turni86 – 883Combined sources
Beta strandi93 – 953Combined sources
Helixi97 – 10812Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi115 – 1217Combined sources
Beta strandi124 – 1307Combined sources
Helixi135 – 1395Combined sources
Beta strandi146 – 1505Combined sources
Helixi160 – 1678Combined sources
Beta strandi174 – 1807Combined sources
Beta strandi186 – 1938Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi202 – 2098Combined sources
Beta strandi212 – 2198Combined sources
Helixi226 – 23914Combined sources
Beta strandi245 – 2484Combined sources
Helixi257 – 2648Combined sources
Turni265 – 2673Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi299 – 3035Combined sources
Helixi310 – 32011Combined sources
Beta strandi325 – 3295Combined sources
Beta strandi336 – 3427Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi348 – 35710Combined sources
Turni365 – 3673Combined sources
Beta strandi372 – 3743Combined sources
Helixi379 – 3835Combined sources
Helixi399 – 41012Combined sources
Beta strandi419 – 4213Combined sources
Helixi424 – 43613Combined sources
Beta strandi443 – 4453Combined sources
Helixi447 – 46216Combined sources
Helixi464 – 4663Combined sources
Helixi468 – 4769Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2CX-ray1.90A44-480[»]
4C2DX-ray2.70A/B/C/D44-480[»]
4C2EX-ray1.80A/B44-480[»]
4C2FX-ray2.40A44-480[»]
4C2GX-ray1.90A44-480[»]
C29-40[»]
4C2HX-ray1.95A/B44-480[»]
ProteinModelPortaliO35002.
SMRiO35002. Positions 54-378, 388-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 18291PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 1164Peptide binding1 Publication

Domaini

The PDZ domain functions as a gatekeeper to the protease tunnel and defines resting and active conformations of the protease.1 Publication

Sequence similaritiesi

Belongs to the peptidase S41A family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CN1. Bacteria.
COG0793. LUCA.
HOGENOMiHOG000038765.
InParanoidiO35002.
OMAiFSSHATE.
PhylomeDBiO35002.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.30.42.10. 1 hit.
3.90.226.10. 2 hits.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001478. PDZ.
IPR004447. Peptidase_S41A.
IPR002477. Peptidoglycan-bd-like.
IPR005151. Tail-specific_protease.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
PF03572. Peptidase_S41. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00245. TSPc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52096. SSF52096. 2 hits.
TIGRFAMsiTIGR00225. prc. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O35002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQKIMAVIA AGSMLFGGAG VYAGINLLEM DKPQTAAVPA TAQADSERDK
60 70 80 90 100
AMDKIEKAYE LISNEYVEKV DREKLLEGAI QGMLSTLNDP YSVYMDKQTA
110 120 130 140 150
KQFSDSLDSS FEGIGAEVGM EDGKIIIVSP FKKSPAEKAG LKPNDEIISI
160 170 180 190 200
NGESMAGKDL NHAVLKIRGK KGSSVSMKIQ RPGTKKQLSF RIKRAEIPLE
210 220 230 240 250
TVFASEKKVQ GHSVGYIAIS TFSEHTAEDF AKALRELEKK EIEGLVIDVR
260 270 280 290 300
GNPGGYLQSV EEILKHFVTK DQPYIQIAER NGDKKRYFST LTHKKAYPVN
310 320 330 340 350
VITDKGSASA SEILAGALKE AGHYDVVGDT SFGKGTVQQA VPMGDGSNIK
360 370 380 390 400
LTLYKWLTPN GNWIHKKGIE PTIAIKQPDY FSAGPLQLKE PLKVDMNNED
410 420 430 440 450
VKHAQVLLKG LSFDPGREDG YFSKDMKKAV MAFQDQNKLN KTGVIDTRTA
460 470 480
ETLNQQIEKK KSDEKNDLQL QTALKSLFVN
Length:480
Mass (Da):52,798
Last modified:January 1, 1998 - v1
Checksum:i902B082C85B5CEC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017113 Genomic DNA. Translation: AAC67263.1.
AL009126 Genomic DNA. Translation: CAB15541.1.
PIRiE70042.
RefSeqiNP_391404.1. NC_000964.3.
WP_003228041.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15541; CAB15541; BSU35240.
GeneIDi936678.
KEGGibsu:BSU35240.
PATRICi18979054. VBIBacSub10457_3689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017113 Genomic DNA. Translation: AAC67263.1.
AL009126 Genomic DNA. Translation: CAB15541.1.
PIRiE70042.
RefSeqiNP_391404.1. NC_000964.3.
WP_003228041.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2CX-ray1.90A44-480[»]
4C2DX-ray2.70A/B/C/D44-480[»]
4C2EX-ray1.80A/B44-480[»]
4C2FX-ray2.40A44-480[»]
4C2GX-ray1.90A44-480[»]
C29-40[»]
4C2HX-ray1.95A/B44-480[»]
ProteinModelPortaliO35002.
SMRiO35002. Positions 54-378, 388-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35002. 3 interactions.
STRINGi224308.Bsubs1_010100019066.

Protein family/group databases

MEROPSiS41.007.
TCDBi9.B.174.1.1. the two tunnel gated c-terminal processing protease (ctp) family.

Proteomic databases

PaxDbiO35002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15541; CAB15541; BSU35240.
GeneIDi936678.
KEGGibsu:BSU35240.
PATRICi18979054. VBIBacSub10457_3689.

Phylogenomic databases

eggNOGiENOG4105CN1. Bacteria.
COG0793. LUCA.
HOGENOMiHOG000038765.
InParanoidiO35002.
OMAiFSSHATE.
PhylomeDBiO35002.

Enzyme and pathway databases

BioCyciBSUB:BSU35240-MONOMER.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.30.42.10. 1 hit.
3.90.226.10. 2 hits.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001478. PDZ.
IPR004447. Peptidase_S41A.
IPR002477. Peptidoglycan-bd-like.
IPR005151. Tail-specific_protease.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
PF03572. Peptidase_S41. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00245. TSPc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52096. SSF52096. 2 hits.
TIGRFAMsiTIGR00225. prc. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCTPB_BACSU
AccessioniPrimary (citable) accession number: O35002
Secondary accession number(s): Q795D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.