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P24327

- PRSA_BACSU

UniProt

P24327 - PRSA_BACSU

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Protein
Foldase protein PrsA
Gene
prsA, BSU09950
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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).UniRule annotation

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: Chromosome

Organism-specific databases

GenoListiBSU09950. [Micado]

Subcellular locationi

Cell membrane; Lipid-anchor Reviewed prediction UniRule annotation

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 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 292273Foldase protein PrsAUniRule annotation
PRO_0000029299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi20 – 201N-palmitoyl cysteine Reviewed prediction
Lipidationi20 – 201S-diacylglycerol cysteine Reviewed prediction

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP24327.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi137 – 14610
Helixi147 – 15913
Helixi163 – 1708
Helixi174 – 1785
Beta strandi181 – 1855
Turni187 – 1893
Helixi195 – 2017
Beta strandi217 – 2248

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZK6NMR-A135-225[»]
ProteinModelPortaliP24327.
SMRiP24327. Positions 135-225.

Miscellaneous databases

EvolutionaryTraceiP24327.

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

Belongs to the PrsA family.
Contains 1 PpiC domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0760.
HOGENOMiHOG000014031.
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

MKKIAIAAIT ATSILALSAC SSGDKEVIAK TDAGDVTKGE LYTNMKKTAG    50
ASVLTQLVQE KVLDKKYKVS DKEIDNKLKE YKTQLGDQYT ALEKQYGKDY 100
LKEQVKYELL TQKAAKDNIK VTDADIKEYW EGLKGKIRAS HILVADKKTA 150
EEVEKKLKKG EKFEDLAKEY STDSSASKGG DLGWFAKEGQ MDETFSKAAF 200
KLKTGEVSDP VKTQYGYHII KKTEERGKYD DMKKELKSEV LEQKLNDNAA 250
VQEAVQKVMK KADIEVKDKD LKDTFNTSST SNSTSSSSSN SK 292
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. Reason: Sequencing errors. The N-terminus of this sequence is probably the N-terminus of phrI.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi S15269.
RefSeqi NP_388876.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZK6 NMR - A 135-225 [» ]
ProteinModelPortali P24327.
SMRi P24327. Positions 135-225.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P24327. 3 interactions.
MINTi MINT-8365681.
STRINGi 224308.BSU09950.

Proteomic databases

PaxDbi P24327.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12835 ; CAB12835 ; BSU09950 .
GeneIDi 939294.
KEGGi bsu:BSU09950.
PATRICi 18973686. VBIBacSub10457_1037.

Organism-specific databases

GenoListi BSU09950. [Micado ]

Phylogenomic databases

eggNOGi COG0760.
HOGENOMi HOG000014031.
KOi K07533.
OMAi MLVEYAV.
OrthoDBi EOG66XBH5.
PhylomeDBi P24327.

Enzyme and pathway databases

BioCyci BSUB:BSU09950-MONOMER.

Miscellaneous databases

EvolutionaryTracei P24327.

Family and domain databases

HAMAPi MF_01145. Foldase_PrsA.
InterProi IPR023059. Foldase_PrsA.
IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR008880. Trigger_fac_C.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view ]
Pfami PF05698. Trigger_C. 1 hit.
[Graphical view ]
SUPFAMi SSF109998. SSF109998. 1 hit.
PROSITEi PS01096. PPIC_PPIASE_1. 1 hit.
PS50198. PPIC_PPIASE_2. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 113 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

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