(data stored in SCRATCH zone)

SWISSPROT: C8U1L0_ECO10

ID   C8U1L0_ECO10            Unreviewed;       246 AA.
AC   C8U1L0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   SubName: Full=Probable pilin chaperone {ECO:0000313|EMBL:BAI29018.1};
GN   OrderedLocusNames=ECO103_0140 {ECO:0000313|EMBL:BAI29018.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29018.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29018.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU003918}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000256|RuleBase:RU003918}.
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DR   EMBL; AP010958; BAI29018.1; -; Genomic_DNA.
DR   RefSeq; WP_000465930.1; NC_013353.1.
DR   SMR; C8U1L0; -.
DR   EnsemblBacteria; BAI29018; BAI29018; ECO103_0140.
DR   KEGG; eoh:ECO103_0140; -.
DR   HOGENOM; HOG000260152; -.
DR   KO; K15540; -.
DR   OMA; KNIVALC; -.
DR   BioCyc; ECOL585395:ECO103_RS00715-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   GO; GO:0043711; P:pilus organization; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1L0.
DR   SWISS-2DPAGE; C8U1L0.
KW   Chaperone {ECO:0000256|RuleBase:RU003918};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    246       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002992691.
FT   DOMAIN       27    152       PapD_N. {ECO:0000259|Pfam:PF00345}.
FT   DOMAIN      177    240       PapD_C. {ECO:0000259|Pfam:PF02753}.
SQ   SEQUENCE   246 AA;  26945 MW;  1EC6CD484DCCCA68 CRC64;
     MFFNTKHTTA LCFVTCMAFS SSSIADIVIS GTRVIYKSDQ KSVNVRLENK GNNPLLVQSW
     LDTGDDNAEP GSITVPFTAT PPVSRIDAKR GQTIKLMYTA STSLPKDRES VFWFNVLEVP
     PKPDAEKVAN QSLLQLAFRT RIKLFYRPDG LKGNPSEAPL ALKWFWSGSE GKASLRVTNP
     TPYYVSFSSG DLEASGKRYP IDVKMIAPFS DEVMKVTGLN GKASSAKVHF YAINDFGGAI
     EGNASL
//

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