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Protein

Serine protease Do-like HtrA

Gene

htrA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable).1 Publication

Catalytic activityi

Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei179Charge relay systemSequence analysis1
Active sitei209Charge relay systemSequence analysis1
Active sitei290Charge relay systemSequence analysis1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciBSUB:BSU12900-MONOMER.

Protein family/group databases

MEROPSiS01.B81.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine protease Do-like HtrA (EC:3.4.21.107)
Alternative name(s):
HtrA-like serine protease
Gene namesi
Name:htrA
Synonyms:ykdA
Ordered Locus Names:BSU12900
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 44CytoplasmicSequence analysisAdd BLAST44
Transmembranei45 – 67HelicalSequence analysisAdd BLAST23
Topological domaini68 – 449ExtracellularSequence analysisAdd BLAST382

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

In contrast to other bacteria, in which inactivation of serine protease leads to thermosensitivity, inactivation of HtrA leads to an increased thermotolerance and an increased tolerance to hydrogen peroxide. Inactivation of both HtrA and HtrB leads to growth defects and to thermosensitivity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000938591 – 449Serine protease Do-like HtrAAdd BLAST449

Proteomic databases

PaxDbiO34358.
PRIDEiO34358.

Expressioni

Inductioni

Transcription is CssS dependent. Induced by heat shock during exponential growth and by heterologous amylases at the transition phase of the growth cycle. Negatively regulates its own expression during exponential growth and during heat shock.3 Publications

Interactioni

Protein-protein interaction databases

IntActiO34358. 3 interactors.
STRINGi224308.Bsubs1_010100007156.

Structurei

3D structure databases

ProteinModelPortaliO34358.
SMRiO34358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini348 – 437PDZPROSITE-ProRule annotationAdd BLAST90

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni288 – 290Substrate bindingBy similarity3
Regioni344 – 348Substrate bindingBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi103 – 108Poly-Ser6
Compositional biasi146 – 152Poly-Ser7

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C0H. Bacteria.
COG0265. LUCA.
HOGENOMiHOG000223641.
InParanoidiO34358.
OMAiWTDEEQE.
PhylomeDBiO34358.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR009003. Peptidase_S1_PA.
IPR001940. Peptidase_S1C.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNYRDENRT KGNENEVFLT KENDQSASYS ARNVIHDQEK KKRGFGWFRP
60 70 80 90 100
LLGGVIGGSL ALGIYTFTPL GDHDSQDTAK QSSSQQQTQS VTATSTSSES
110 120 130 140 150
KKSSSSSSAF KSEDSSKISD MVEDLSPAIV GITNLQAQSN SSLFGSSSSD
160 170 180 190 200
SSEDTESGSG SGVIFKKENG KAYIITNNHV VEGASSLKVS LYDGTEVTAK
210 220 230 240 250
LVGSDSLTDL AVLQISDDHV TKVANFGDSS DLRTGETVIA IGDPLGKDLS
260 270 280 290 300
RTVTQGIVSG VDRTVSMSTS AGETSINVIQ TDAAINPGNS GGPLLNTDGK
310 320 330 340 350
IVGINSMKIS EDDVEGIGFA IPSNDVKPIA EELLSKGQIE RPYIGVSMLD
360 370 380 390 400
LEQVPQNYQE GTLGLFGSQL NKGVYIREVA SGSPAEKAGL KAEDIIIGLK
410 420 430 440
GKEIDTGSEL RNILYKDAKI GDTVEVKILR NGKEMTKKIK LDQKEEKTS
Length:449
Mass (Da):47,715
Last modified:June 16, 2009 - v2
Checksum:i8E4A28CDE18C4612
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti72D → N in CAA05570 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002571 Genomic DNA. Translation: CAA05570.1.
AL009126 Genomic DNA. Translation: CAB13147.2.
PIRiA69643.
RefSeqiNP_389173.2. NC_000964.3.
WP_009967069.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13147; CAB13147; BSU12900.
GeneIDi939849.
KEGGibsu:BSU12900.
PATRICi18974335. VBIBacSub10457_1360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002571 Genomic DNA. Translation: CAA05570.1.
AL009126 Genomic DNA. Translation: CAB13147.2.
PIRiA69643.
RefSeqiNP_389173.2. NC_000964.3.
WP_009967069.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO34358.
SMRiO34358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO34358. 3 interactors.
STRINGi224308.Bsubs1_010100007156.

Protein family/group databases

MEROPSiS01.B81.

Proteomic databases

PaxDbiO34358.
PRIDEiO34358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13147; CAB13147; BSU12900.
GeneIDi939849.
KEGGibsu:BSU12900.
PATRICi18974335. VBIBacSub10457_1360.

Phylogenomic databases

eggNOGiENOG4105C0H. Bacteria.
COG0265. LUCA.
HOGENOMiHOG000223641.
InParanoidiO34358.
OMAiWTDEEQE.
PhylomeDBiO34358.

Enzyme and pathway databases

BioCyciBSUB:BSU12900-MONOMER.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR009003. Peptidase_S1_PA.
IPR001940. Peptidase_S1C.
[Graphical view]
PfamiPF13180. PDZ_2. 1 hit.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHTRA_BACSU
AccessioniPrimary (citable) accession number: O34358
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: June 16, 2009
Last modified: November 2, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Inactivation results in compensating overexpression of YtvA, especially during stress conditions.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Peptidase families
    Classification of peptidase families and list of entries
  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.