(data stored in SCRATCH zone)

SWISSPROT: A0A152UP93_ECO57

ID   A0A152UP93_ECO57        Unreviewed;       241 AA.
AC   A0A152UP93; A0A0H3JC13;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-JUL-2017, entry version 10.
DE   SubName: Full=Probable pilin chaperone {ECO:0000313|EMBL:BAB33567.1};
GN   OrderedLocusNames=ECs0144 {ECO:0000313|EMBL:BAB33567.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33567.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33567.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; BA000007; BAB33567.1; -; Genomic_DNA.
DR   RefSeq; NP_308171.1; NC_002695.1.
DR   RefSeq; WP_000484311.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; A0A152UP93; -.
DR   EnsemblBacteria; BAB33567; BAB33567; BAB33567.
DR   GeneID; 913756; -.
DR   KEGG; ecs:ECs0144; -.
DR   PATRIC; fig|386585.9.peg.243; -.
DR   KO; K15540; -.
DR   Proteomes; UP000000558; 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.
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; A0A152UP93.
DR   SWISS-2DPAGE; A0A152UP93.
KW   Chaperone {ECO:0000256|RuleBase:RU003918,
KW   ECO:0000256|SAAS:SAAS00758229};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    241       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5009815357.
FT   DOMAIN       27    150       PapD_N. {ECO:0000259|Pfam:PF00345}.
FT   DOMAIN      173    234       PapD_C. {ECO:0000259|Pfam:PF02753}.
SQ   SEQUENCE   241 AA;  26317 MW;  061046CD7DEF7602 CRC64;
     MFPLVKKTVS ALFVSTLLAS APAFADIIIS GTRIIYNADK KDVNVRLENK GNRPLLIQNW
     LDTGDDNADP SQIKVPFTAT PPVSRVEPKR GQTVKVMYTG ATALPKDRES VYWFNVLEVP
     PKPKDAEADK NLLQLAFRTR IKLFYRPSGL QGEPAEAPAK ITWKLNNAQL QANNPTPYYV
     SFNEVKLESG GKTYNVNSSM VTPFSQASFG VTSLPGSVSS GKVVFKAIND FGGNIDGSAT
     F
//

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