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P24327 (PRSA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Foldase protein PrsA

EC=5.2.1.8
Gene names
Name:prsA
Ordered Locus Names:BSU09950
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential protein that plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Has PPIase activity but it is not essential for its function in vivo. Ref.6

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). HAMAP-Rule MF_01145

Subcellular location

Cell membrane; Lipid-anchor Potential HAMAP-Rule MF_01145.

Domain

All three domains (PPIase domain and the flanking N- and C-terminal domains) are essential for activity. HAMAP-Rule MF_01145

Sequence similarities

Belongs to the PrsA family.

Contains 1 PpiC domain.

Sequence caution

The sequence AAA22825.1 differs from that shown. Reason: Sequencing errors. The N-terminus of this sequence is probably the N-terminus of phrI.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionIsomerase
Rotamase
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 292273Foldase protein PrsA HAMAP-Rule MF_01145
PRO_0000029299

Regions

Domain134 – 22491PpiC

Amino acid modifications

Lipidation201N-palmitoyl cysteine Potential
Lipidation201S-diacylglycerol cysteine Potential

Experimental info

Mutagenesis201C → Y: Abolishes lipid modification of the protein. Ref.8
Mutagenesis1411H → A: Loss of PPIase function. No effect on secretion of proteins and on growth. Ref.7
Mutagenesis1631F → Y: No effect on secretion of proteins and on growth. Ref.7
Mutagenesis1711S → A: No effect on secretion of proteins and on growth. Ref.7
Mutagenesis1731D → A: Decrease in PPIase activity. No effect on secretion of proteins and on growth. Ref.7
Mutagenesis1751S → P: No effect on secretion of proteins and on growth.
Mutagenesis1801G → A: No effect on secretion of proteins and on growth. Ref.7
Mutagenesis1911M → A: No effect on secretion of proteins and on growth. Ref.7
Mutagenesis1951F → A or Y: No effect on secretion of proteins and on growth. Ref.7
Mutagenesis2151Y → A: No effect on secretion of proteins and on growth. Ref.7
Mutagenesis2161G → A: Decreased secretion of proteins; no effect on growth. Ref.7
Mutagenesis2181H → A: Decreased secretion of proteins; no effect on growth. Ref.7
Mutagenesis2191I → A: No effect on secretion of proteins and on growth. Ref.7

Secondary structure

................ 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24327 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: DEC194D8FE5C9FC0

FASTA29232,510
        10         20         30         40         50         60 
MKKIAIAAIT ATSILALSAC SSGDKEVIAK TDAGDVTKGE LYTNMKKTAG ASVLTQLVQE 

        70         80         90        100        110        120 
KVLDKKYKVS DKEIDNKLKE YKTQLGDQYT ALEKQYGKDY LKEQVKYELL TQKAAKDNIK 

       130        140        150        160        170        180 
VTDADIKEYW EGLKGKIRAS HILVADKKTA EEVEKKLKKG EKFEDLAKEY STDSSASKGG 

       190        200        210        220        230        240 
DLGWFAKEGQ MDETFSKAAF KLKTGEVSDP VKTQYGYHII KKTEERGKYD DMKKELKSEV 

       250        260        270        280        290 
LEQKLNDNAA VQEAVQKVMK KADIEVKDKD LKDTFNTSST SNSTSSSSSN SK 

« Hide

References

« Hide 'large scale' references
[1]"A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export."
Kontinen V.P., Saris P., Sarvas M.
Mol. Microbiol. 5:1273-1283(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Characterization of signal-sequence-coding regions selected from the Bacillus subtilis chromosome."
Smith H., de Jong A., Bron S., Venema G.
Gene 70:351-361(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-210.
[5]"Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis."
Vitikainen M., Pummi T., Airaksinen U., Wahlstroem E., Wu H., Sarvas M., Kontinen V.P.
J. Bacteriol. 183:1881-1890(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 168.
[6]"The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis."
Wahlstroem E., Vitikainen M., Kontinen V.P., Sarvas M.
Microbiology 149:569-577(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE CELL WALL.
Strain: 168.
[7]"Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis."
Vitikainen M., Lappalainen I., Seppala R., Antelmann H., Boer H., Taira S., Savilahti H., Hecker M., Vihinen M., Sarvas M., Kontinen V.P.
J. Biol. Chem. 279:19302-19314(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-141; PHE-163; SER-171; ASP-173; GLY-180; MET-191; PHE-195; TYR-215; GLY-216; HIS-218 AND ILE-219.
Strain: 168.
[8]"Mutants of Bacillus subtilis defective in protein export."
Kontinen V.P., Sarvas M.
J. Gen. Microbiol. 134:2333-2344(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-20.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57271 Genomic DNA. Translation: CAA40543.1.
Y14077 Genomic DNA. Translation: CAA74418.1.
AL009126 Genomic DNA. Translation: CAB12835.1.
M22909 Genomic DNA. Translation: AAA22825.1. Sequence problems.
PIRS15269.
RefSeqNP_388876.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZK6NMR-A135-225[»]
ProteinModelPortalP24327.
SMRP24327. Positions 135-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24327. 3 interactions.
MINTMINT-8365681.
STRING224308.BSU09950.

Proteomic databases

PaxDbP24327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12835; CAB12835; BSU09950.
GeneID939294.
KEGGbsu:BSU09950.
PATRIC18973686. VBIBacSub10457_1037.

Organism-specific databases

GenoListBSU09950. [Micado]

Phylogenomic databases

eggNOGCOG0760.
HOGENOMHOG000014031.
KOK07533.
OMAMLVEYAV.
OrthoDBEOG66XBH5.
ProtClustDBCLSK886987.

Enzyme and pathway databases

BioCycBSUB:BSU09950-MONOMER.

Family and domain databases

HAMAPMF_01145. Foldase_PrsA.
InterProIPR023059. Foldase_PrsA.
IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR008880. Trigger_fac_C.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamPF05698. Trigger_C. 1 hit.
[Graphical view]
SUPFAMSSF109998. SSF109998. 1 hit.
PROSITEPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24327.

Entry information

Entry namePRSA_BACSU
AccessionPrimary (citable) accession number: P24327
Secondary accession number(s): Q45680
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList