ID   F3WK18_9ENTR            Unreviewed;       214 AA.
AC   F3WK18;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   15-FEB-2017, entry version 22.
DE   SubName: Full=Chaperone protein pmfD {ECO:0000313|EMBL:EGI93588.1};
GN   ORFNames=SB521682_2720 {ECO:0000313|EMBL:EGI93588.1};
OS   Shigella boydii 5216-82.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=766141 {ECO:0000313|EMBL:EGI93588.1, ECO:0000313|Proteomes:UP000004081};
RN   [1] {ECO:0000313|EMBL:EGI93588.1, ECO:0000313|Proteomes:UP000004081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5216-82 {ECO:0000313|EMBL:EGI93588.1,
RC   ECO:0000313|Proteomes:UP000004081};
RA   Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L.,
RA   Jones K., Santana-Cruz I., Liu X.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU003918}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000256|RuleBase:RU003918}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGI93588.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFGE01000044; EGI93588.1; -; Genomic_DNA.
DR   RefSeq; WP_000602545.1; NZ_AFGE01000044.1.
DR   EnsemblBacteria; EGI93588; EGI93588; SB521682_2720.
DR   PATRIC; 53849198; VBIShiBoy163146_2706.
DR   OrthoDB; POG091H0HZS; -.
DR   Proteomes; UP000004081; Unassembled WGS sequence.
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; 2.60.40.1070; -; 1.
DR   Gene3D; 2.60.40.360; -; 1.
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;
KW   Chaperone {ECO:0000256|RuleBase:RU003918};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004081}.
FT   DOMAIN        2    111       PapD_N. {ECO:0000259|Pfam:PF00345}.
FT   DOMAIN      135    192       PapD_C. {ECO:0000259|Pfam:PF02753}.
SQ   SEQUENCE   214 AA;  24074 MW;  C730C2FCFF9B19D1 CRC64;
     MILNESDKSI SVTLRNNDPK LPYLAQSWIE DEKGNKISSP LTVLPPVQRI DSMMNGQVKV
     QGMPDINKLP ADRESLFYFN VREIPPKSNK VNTLQIALQT RIKLFWRPKA LENVSMKNPW
     QYKVTLTRNG QEFTVNNPTP YYVIFSNAST QKNGNPAAGF SPIVMSPKTS APLNVKMGSV
     PVLTYVNDYG ARMPLFFTCN GNSCQVDEEQ SRKG
//