PRSA_BACSU
ID PRSA_BACSU Reviewed; 292 AA.
AC P24327; Q45680;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Foldase protein PrsA;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA; OrderedLocusNames=BSU09950;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1956302; DOI=10.1111/j.1365-2958.1991.tb01901.x;
RA Kontinen V.P., Saris P., Sarvas M.;
RT "A gene (prsA) of Bacillus subtilis involved in a novel, late stage of
RT protein export.";
RL Mol. Microbiol. 5:1273-1283(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-210.
RX PubMed=3145906; DOI=10.1016/0378-1119(88)90207-7;
RA Smith H., de Jong A., Bron S., Venema G.;
RT "Characterization of signal-sequence-coding regions selected from the
RT Bacillus subtilis chromosome.";
RL Gene 70:351-361(1988).
RN [5]
RP CHARACTERIZATION.
RC STRAIN=168;
RX PubMed=11222585; DOI=10.1128/jb.183.6.1881-1890.2001;
RA Vitikainen M., Pummi T., Airaksinen U., Wahlstroem E., Wu H., Sarvas M.,
RA Kontinen V.P.;
RT "Quantitation of the capacity of the secretion apparatus and requirement
RT for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis.";
RL J. Bacteriol. 183:1881-1890(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH THE CELL WALL.
RC STRAIN=168;
RX PubMed=12634326; DOI=10.1099/mic.0.25511-0;
RA Wahlstroem E., Vitikainen M., Kontinen V.P., Sarvas M.;
RT "The extracytoplasmic folding factor PrsA is required for protein secretion
RT only in the presence of the cell wall in Bacillus subtilis.";
RL Microbiology 149:569-577(2003).
RN [7]
RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-141; PHE-163; SER-171; ASP-173;
RP SER-175; GLY-180; MET-191; PHE-195; TYR-215; GLY-216; HIS-218 AND ILE-219.
RC STRAIN=168;
RX PubMed=14976191; DOI=10.1074/jbc.m400861200;
RA Vitikainen M., Lappalainen I., Seppala R., Antelmann H., Boer H., Taira S.,
RA Savilahti H., Hecker M., Vihinen M., Sarvas M., Kontinen V.P.;
RT "Structure-function analysis of PrsA reveals roles for the parvulin-like
RT and flanking N- and C-terminal domains in protein folding and secretion in
RT Bacillus subtilis.";
RL J. Biol. Chem. 279:19302-19314(2004).
RN [8]
RP MUTAGENESIS OF CYS-20.
RX PubMed=3150980; DOI=10.1099/00221287-134-8-2333;
RA Kontinen V.P., Sarvas M.;
RT "Mutants of Bacillus subtilis defective in protein export.";
RL J. Gen. Microbiol. 134:2333-2344(1988).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
CC -!- FUNCTION: Essential protein that plays a major role in protein
CC secretion by helping the post-translocational extracellular folding of
CC several secreted proteins. Has PPIase activity but it is not essential
CC for its function in vivo. {ECO:0000269|PubMed:12634326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210, ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC Membrane raft {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}; Lipid-anchor {ECO:0000305}. Note=Present
CC in detergent-resistant membrane (DRM) fractions that may be equivalent
CC to eukaryotic membrane rafts; these rafts include proteins involved in
CC signaling, molecule trafficking and protein secretion.
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}.
CC -!- DOMAIN: All three domains (PPIase domain and the flanking N- and C-
CC terminal domains) are essential for activity.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22825.1; Type=Miscellaneous discrepancy; Note=Sequencing errors. The N-terminus of this sequence is probably the N-terminus of phrI.; Evidence={ECO:0000305};
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DR EMBL; X57271; CAA40543.1; -; Genomic_DNA.
DR EMBL; Y14077; CAA74418.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12835.1; -; Genomic_DNA.
DR EMBL; M22909; AAA22825.1; ALT_SEQ; Genomic_DNA.
DR PIR; S15269; S15269.
DR RefSeq; NP_388876.1; NC_000964.3.
DR RefSeq; WP_003245079.1; NZ_JNCM01000035.1.
DR PDB; 1ZK6; NMR; -; A=135-225.
DR PDB; 4WO7; X-ray; 2.63 A; A/B=21-280.
DR PDBsum; 1ZK6; -.
DR PDBsum; 4WO7; -.
DR AlphaFoldDB; P24327; -.
DR SMR; P24327; -.
DR IntAct; P24327; 3.
DR MINT; P24327; -.
DR STRING; 224308.BSU09950; -.
DR MEROPS; M67.A10; -.
DR jPOST; P24327; -.
DR PaxDb; P24327; -.
DR PRIDE; P24327; -.
DR EnsemblBacteria; CAB12835; CAB12835; BSU_09950.
DR GeneID; 939294; -.
DR KEGG; bsu:BSU09950; -.
DR PATRIC; fig|224308.179.peg.1068; -.
DR eggNOG; COG0760; Bacteria.
DR InParanoid; P24327; -.
DR OMA; TMKGSTI; -.
DR PhylomeDB; P24327; -.
DR BioCyc; BSUB:BSU09950-MON; -.
DR EvolutionaryTrace; P24327; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 1.10.3120.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR HAMAP; MF_01145; Foldase_PrsA; 1.
DR InterPro; IPR023059; Foldase_PrsA.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR SUPFAM; SSF109998; SSF109998; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..292
FT /note="Foldase protein PrsA"
FT /id="PRO_0000029299"
FT DOMAIN 134..224
FT /note="PpiC"
FT REGION 270..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT MUTAGEN 20
FT /note="C->Y: Abolishes lipid modification of the protein."
FT /evidence="ECO:0000269|PubMed:3150980"
FT MUTAGEN 141
FT /note="H->A: Loss of PPIase function. No effect on
FT secretion of proteins and on growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 163
FT /note="F->Y: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 171
FT /note="S->A: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 173
FT /note="D->A: Decrease in PPIase activity. No effect on
FT secretion of proteins and on growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 175
FT /note="S->P: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 180
FT /note="G->A: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 191
FT /note="M->A: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 195
FT /note="F->A,Y: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 215
FT /note="Y->A: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 216
FT /note="G->A: Decreased secretion of proteins; no effect on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 218
FT /note="H->A: Decreased secretion of proteins; no effect on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT MUTAGEN 219
FT /note="I->A: No effect on secretion of proteins and on
FT growth."
FT /evidence="ECO:0000269|PubMed:14976191"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4WO7"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 38..66
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:4WO7"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4WO7"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:4WO7"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:4WO7"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:4WO7"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:4WO7"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:4WO7"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:4WO7"
SQ SEQUENCE 292 AA; 32510 MW; DEC194D8FE5C9FC0 CRC64;
MKKIAIAAIT ATSILALSAC SSGDKEVIAK TDAGDVTKGE LYTNMKKTAG ASVLTQLVQE
KVLDKKYKVS DKEIDNKLKE YKTQLGDQYT ALEKQYGKDY LKEQVKYELL TQKAAKDNIK
VTDADIKEYW EGLKGKIRAS HILVADKKTA EEVEKKLKKG EKFEDLAKEY STDSSASKGG
DLGWFAKEGQ MDETFSKAAF KLKTGEVSDP VKTQYGYHII KKTEERGKYD DMKKELKSEV
LEQKLNDNAA VQEAVQKVMK KADIEVKDKD LKDTFNTSST SNSTSSSSSN SK
