ID PPID_ECOL6 Reviewed; 623 AA.
AC P0ADY2; P77241;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 30-NOV-2016, entry version 74.
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; OrderedLocusNames=c0557;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence
RT of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. Seems to be
CC involved in the folding of outer membrane proteins (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}; Periplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Contains 1 PpiC domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00278}.
DR EMBL; AE014075; AAN79035.1; -; Genomic_DNA.
DR RefSeq; WP_000969372.1; NC_004431.1.
DR ProteinModelPortal; P0ADY2; -.
DR SMR; P0ADY2; -.
DR STRING; 199310.c0557; -.
DR EnsemblBacteria; AAN79035; AAN79035; c0557.
DR KEGG; ecc:c0557; -.
DR PATRIC; 18279154; VBIEscCol75197_0522.
DR eggNOG; ENOG4105EIN; Bacteria.
DR eggNOG; COG0760; LUCA.
DR HOGENOM; HOG000276975; -.
DR KO; K03770; -.
DR OMA; DQVIRQM; -.
DR BioCyc; ECOL199310:C0557-MONOMER; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR Gene3D; 1.10.3120.10; -; 1.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR008880; Trigger_fac_C.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Complete proteome; Isomerase;
KW Membrane; Rotamase; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 623 Peptidyl-prolyl cis-trans isomerase D.
FT /FTId=PRO_0000193424.
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}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 266 355 iprf:PPIC_PPIASE_2 [T]
FT MYHIT 295 316 ipat:PPIC_PPIASE_1 [T]
FT MYHIT 247 369 ipfam:Rotamase_2 [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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