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Protein

Foldase protein PrsA

Gene

prsA

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

Functioni

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.1 Publication

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. protein folding Source: UniProtKB-HAMAP
  2. protein transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

BioCyciBSUB:BSU09950-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Foldase protein PrsA (EC:5.2.1.8)
Gene namesi
Name:prsA
Ordered Locus Names:BSU09950
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU09950. [Micado]

Subcellular locationi

  1. Cell membrane Curated; Lipid-anchor Curated

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201C → Y: Abolishes lipid modification of the protein. 1 Publication
Mutagenesisi141 – 1411H → A: Loss of PPIase function. No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi163 – 1631F → Y: No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi171 – 1711S → A: No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi173 – 1731D → A: Decrease in PPIase activity. No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi175 – 1751S → P: No effect on secretion of proteins and on growth.
Mutagenesisi180 – 1801G → A: No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi191 – 1911M → A: No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi195 – 1951F → A or Y: No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi215 – 2151Y → A: No effect on secretion of proteins and on growth. 1 Publication
Mutagenesisi216 – 2161G → A: Decreased secretion of proteins; no effect on growth. 1 Publication
Mutagenesisi218 – 2181H → A: Decreased secretion of proteins; no effect on growth. 1 Publication
Mutagenesisi219 – 2191I → A: No effect on secretion of proteins and on growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 292273Foldase protein PrsAPRO_0000029299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi20 – 201N-palmitoyl cysteineSequence Analysis
Lipidationi20 – 201S-diacylglycerol cysteineSequence Analysis

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP24327.

Interactioni

Protein-protein interaction databases

IntActiP24327. 3 interactions.
MINTiMINT-8365681.
STRINGi224308.BSU09950.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 253Combined sources
Beta strandi27 – 315Combined sources
Helixi38 – 6629Combined sources
Helixi71 – 8414Combined sources
Helixi88 – 958Combined sources
Helixi98 – 11821Combined sources
Helixi123 – 1308Combined sources
Beta strandi136 – 14510Combined sources
Helixi147 – 15913Combined sources
Helixi163 – 1708Combined sources
Helixi174 – 1763Combined sources
Turni177 – 1804Combined sources
Beta strandi181 – 19111Combined sources
Helixi193 – 2008Combined sources
Beta strandi217 – 2248Combined sources
Turni229 – 2313Combined sources
Helixi233 – 24513Combined sources
Helixi248 – 26114Combined sources
Helixi269 – 2713Combined sources
Turni272 – 2765Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZK6NMR-A135-225[»]
4WO7X-ray2.63A/B21-280[»]
SMRiP24327. Positions 135-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 22491PpiCAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the PrsA family.Curated
Contains 1 PpiC domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0760.
HOGENOMiHOG000014031.
InParanoidiP24327.
KOiK07533.
OMAiMLVEYAV.
OrthoDBiEOG66XBH5.
PhylomeDBiP24327.

Family and domain databases

HAMAPiMF_01145. Foldase_PrsA.
InterProiIPR023059. Foldase_PrsA.
IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR008880. Trigger_fac_C.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF05698. Trigger_C. 1 hit.
[Graphical view]
SUPFAMiSSF109998. SSF109998. 1 hit.
PROSITEiPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIAIAAIT ATSILALSAC SSGDKEVIAK TDAGDVTKGE LYTNMKKTAG
60 70 80 90 100
ASVLTQLVQE KVLDKKYKVS DKEIDNKLKE YKTQLGDQYT ALEKQYGKDY
110 120 130 140 150
LKEQVKYELL TQKAAKDNIK VTDADIKEYW EGLKGKIRAS HILVADKKTA
160 170 180 190 200
EEVEKKLKKG EKFEDLAKEY STDSSASKGG DLGWFAKEGQ MDETFSKAAF
210 220 230 240 250
KLKTGEVSDP VKTQYGYHII KKTEERGKYD DMKKELKSEV LEQKLNDNAA
260 270 280 290
VQEAVQKVMK KADIEVKDKD LKDTFNTSST SNSTSSSSSN SK
Length:292
Mass (Da):32,510
Last modified:March 1, 1992 - v1
Checksum:iDEC194D8FE5C9FC0
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS15269.
RefSeqiNP_388876.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12835; CAB12835; BSU09950.
GeneIDi939294.
KEGGibsu:BSU09950.
PATRICi18973686. VBIBacSub10457_1037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS15269.
RefSeqiNP_388876.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZK6NMR-A135-225[»]
4WO7X-ray2.63A/B21-280[»]
SMRiP24327. Positions 135-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP24327. 3 interactions.
MINTiMINT-8365681.
STRINGi224308.BSU09950.

Proteomic databases

PaxDbiP24327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12835; CAB12835; BSU09950.
GeneIDi939294.
KEGGibsu:BSU09950.
PATRICi18973686. VBIBacSub10457_1037.

Organism-specific databases

GenoListiBSU09950. [Micado]

Phylogenomic databases

eggNOGiCOG0760.
HOGENOMiHOG000014031.
InParanoidiP24327.
KOiK07533.
OMAiMLVEYAV.
OrthoDBiEOG66XBH5.
PhylomeDBiP24327.

Enzyme and pathway databases

BioCyciBSUB:BSU09950-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP24327.

Family and domain databases

HAMAPiMF_01145. Foldase_PrsA.
InterProiIPR023059. Foldase_PrsA.
IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR008880. Trigger_fac_C.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF05698. Trigger_C. 1 hit.
[Graphical view]
SUPFAMiSSF109998. SSF109998. 1 hit.
PROSITEiPS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPRSA_BACSU
AccessioniPrimary (citable) accession number: P24327
Secondary accession number(s): Q45680
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 1, 2015
This is version 119 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.