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P24327

- PRSA_BACSU

UniProt

P24327 - PRSA_BACSU

Protein

Foldase protein PrsA

Gene

prsA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    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

    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 Curated; Lipid-anchor Curated

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    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
    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.
    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.
    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

    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: October 1, 2014
    This is version 114 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