ID PPID_ECOLI Reviewed; 623 AA.
AC P0ADY1; P77241; Q2MBY5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 10-MAY-2017, entry version 92.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE Short=PPIase D;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase D;
GN Name=ppiD; Synonyms=ybaU; OrderedLocusNames=b0441, JW0431;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS.
RX PubMed=9670013; DOI=10.1093/emboj/17.14.3968;
RA Dartigalongue C., Raina S.;
RT "A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase
RT required for folding of outer membrane proteins in Escherichia coli.";
RL EMBO J. 17:3968-3980(1998).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.M506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. Seems to be
CC involved in the folding of outer membrane proteins. Its preference
CC at the P1 position of the peptide substrate is Glu > Leu > Ala >
CC His > Val > Phe > Ile > Gly > Lys > Thr.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBUNIT: Has been isolated as a homodimer and homotrimer from
CC inner membrane preparations. {ECO:0000269|PubMed:16079137}.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-562001, EBI-562001;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16079137}; Single-pass type II membrane
CC protein {ECO:0000269|PubMed:16079137}; Periplasmic side
CC {ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: By heat shock.
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DR EMBL; D82943; BAA11645.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40197.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73544.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76221.1; -; Genomic_DNA.
DR PIR; A64774; A64774.
DR RefSeq; NP_414975.1; NC_000913.3.
DR RefSeq; WP_000969372.1; NZ_LN832404.1.
DR PDB; 2KGJ; NMR; -; A=264-357.
DR PDBsum; 2KGJ; -.
DR ProteinModelPortal; P0ADY1; -.
DR SMR; P0ADY1; -.
DR BioGrid; 4260732; 132.
DR DIP; DIP-39902N; -.
DR IntAct; P0ADY1; 8.
DR STRING; 511145.b0441; -.
DR EPD; P0ADY1; -.
DR PaxDb; P0ADY1; -.
DR PRIDE; P0ADY1; -.
DR EnsemblBacteria; AAC73544; AAC73544; b0441.
DR EnsemblBacteria; BAE76221; BAE76221; BAE76221.
DR GeneID; 946056; -.
DR KEGG; ecj:JW0431; -.
DR KEGG; eco:b0441; -.
DR PATRIC; 32116035; VBIEscCol129921_0459.
DR EchoBASE; EB3038; -.
DR EcoGene; EG13249; ppiD.
DR eggNOG; ENOG4105EIN; Bacteria.
DR eggNOG; COG0760; LUCA.
DR HOGENOM; HOG000276975; -.
DR InParanoid; P0ADY1; -.
DR KO; K03770; -.
DR OMA; DQVIRQM; -.
DR PhylomeDB; P0ADY1; -.
DR BioCyc; EcoCyc:G6242-MONOMER; -.
DR EvolutionaryTrace; P0ADY1; -.
DR PRO; PR:P0ADY1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR027304; Trigger_fact/SurA_dom.
DR Pfam; PF13145; Rotamase_2; 1.
DR SUPFAM; SSF109998; SSF109998; 2.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
KW Isomerase; Membrane; Reference proteome; Rotamase; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 623 Peptidyl-prolyl cis-trans isomerase D.
FT /FTId=PRO_0000193423.
FT TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 16 36 Helical. {ECO:0000255}.
FT TOPO_DOM 37 623 Periplasmic. {ECO:0000255}.
FT DOMAIN 266 355 PpiC. {ECO:0000255|PROSITE-
FT ProRule:PRU00278}.
FT MUTAGEN 312 312 G->A,R: Loss of activity.
FT {ECO:0000269|PubMed:9670013}.
FT MUTAGEN 313 313 G->A,R: Loss of activity.
FT {ECO:0000269|PubMed:9670013}.
FT MUTAGEN 347 347 G->A: Loss of activity.
FT {ECO:0000269|PubMed:9670013}.
FT MUTAGEN 350 350 I->A,F: Loss of activity.
FT {ECO:0000269|PubMed:9670013}.
FT STRAND 268 278 {ECO:0000244|PDB:2KGJ}.
FT HELIX 279 291 {ECO:0000244|PDB:2KGJ}.
FT HELIX 295 301 {ECO:0000244|PDB:2KGJ}.
FT HELIX 306 309 {ECO:0000244|PDB:2KGJ}.
FT TURN 310 312 {ECO:0000244|PDB:2KGJ}.
FT STRAND 313 319 {ECO:0000244|PDB:2KGJ}.
FT HELIX 325 328 {ECO:0000244|PDB:2KGJ}.
FT STRAND 338 344 {ECO:0000244|PDB:2KGJ}.
FT STRAND 347 357 {ECO:0000244|PDB:2KGJ}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 247 369 ipfam:Rotamase_2 [T]
FT MYHIT 266 355 iprf:PPIC_PPIASE_2 [T]
FT MYHIT 295 316 ipat:PPIC_PPIASE_1 [T]
SQ SEQUENCE 623 AA; 68150 MW; 0F646F687114A387 CRC64;
MMDSLRTAAN SLVLKIIFGI IIVSFILTGV SGYLIGGGNN YAAKVNDQEI SRGQFENAFN
SERNRMQQQL GDQYSELAAN EGYMKTLRQQ VLNRLIDEAL LDQYARELKL GISDEQVKQA
IFATPAFQVD GKFDNSRYNG ILNQMGMTAD QYAQALRNQL TTQQLINGVA GTDFMLKGET
DELAALVAQQ RVVREATIDV NALAAKQPVT EQEIASYYEQ NKNNFMTPEQ FRVSYIKLDA
ATMQQPVSDA DIQSYYDQHQ DQFTQPQRTR YSIIQTKTED EAKAVLDELN KGGDFAALAK
EKSADIISAR NGGDMGWLED ATIPDELKNA GLKEKGQLSG VIKSSVGFLI VRLDDIQPAK
VKSLDEVRDD IAAKVKHEKA LDAYYALQQK VSDAASNDTE SLAGAEQAAG VKATQTGWFS
KDNLPEELNF KPVADAIFNG GLVGENGAPG INSDIITVDG DRAFVLRISE HKPEAVKPLA
DVQEQVKALV QHNKAEQQAK VDAEKLLVDL KAGKGAEAMQ AAGLKFGEPK TLSRSGRDPI
SQAAFALPLP AKDKPSYGMA TDMQGNVVLL ALDEVKQGSM PEDQKKAMVQ GITQNNAQIV
FEALMSNLRK EAKIKIGDAL EQQ
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