PAPC_ECOLX
ID PAPC_ECOLX Reviewed; 836 AA.
AC P07110; Q8RNL0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Outer membrane usher protein PapC;
DE Flags: Precursor;
GN Name=papC;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=2897064; DOI=10.1111/j.1365-2958.1987.tb00509.x;
RA Norgren M., Baga M., Tennent J.M., Normark S.;
RT "Nucleotide sequence, regulation and functional analysis of the papC gene
RT required for cell surface localization of Pap pili of uropathogenic
RT Escherichia coli.";
RL Mol. Microbiol. 1:169-178(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=1357526; DOI=10.1111/j.1365-2958.1992.tb01399.x;
RA Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M., Lindberg F.,
RA Gaastra W., Normark S.;
RT "Horizontal gene transfer of the Escherichia coli pap and prs pili operons
RT as a mechanism for the development of tissue-specific adhesive
RT properties.";
RL Mol. Microbiol. 6:2225-2242(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 517-543.
RX PubMed=12399496; DOI=10.1128/jb.184.22.6260-6269.2002;
RA Thanassi D.G., Stathopoulos C., Dodson K., Geiger D., Hultgren S.J.;
RT "Bacterial outer membrane ushers contain distinct targeting and assembly
RT domains for pilus biogenesis.";
RL J. Bacteriol. 184:6260-6269(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 720-836.
RX PubMed=2572580; DOI=10.1128/jb.171.11.6052-6058.1989;
RA Lindberg F., Tennent J.M., Hultgren S.J., Lund B., Normark S.;
RT "PapD, a periplasmic transport protein in P-pilus biogenesis.";
RL J. Bacteriol. 171:6052-6058(1989).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7909802; DOI=10.1016/s0021-9258(18)99895-9;
RA Jacob-Dubuisson F., Striker R., Hultgren S.J.;
RT "Chaperone-assisted self-assembly of pili independent of cellular energy.";
RL J. Biol. Chem. 269:12447-12455(1994).
RN [6]
RP SUBUNIT.
RX PubMed=9501230; DOI=10.1073/pnas.95.6.3146;
RA Thanassi D.G., Saulino E.T., Lombardo M.J., Roth R., Heuser J.,
RA Hultgren S.J.;
RT "The PapC usher forms an oligomeric channel: implications for pilus
RT biogenesis across the outer membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3146-3151(1998).
CC -!- FUNCTION: Involved in the export and assembly of pili subunits across
CC the outer membrane. Forms a hexameric ring-shaped pore in the outer
CC bacterial membrane. The 2 nanometer-diameter pore allows the passage of
CC the thin tip fibrillum. As for the rod, it probably unwinds into linear
CC fibers which would therefore be narrow enough to pass through the pore.
CC -!- INTERACTION:
CC P07110; P07110: papC; NbExp=3; IntAct=EBI-15770957, EBI-15770957;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the fimbrial export usher family. {ECO:0000305}.
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; Y00529; CAA68588.1; -; Genomic_DNA.
DR EMBL; X61239; CAA43564.1; -; Genomic_DNA.
DR EMBL; AF481883; AAL89688.1; -; Genomic_DNA.
DR PIR; S25218; S25218.
DR PDB; 2KT6; NMR; -; A=752-836.
DR PDB; 2VQI; X-ray; 3.20 A; A/B=157-667.
DR PDB; 3FIP; X-ray; 3.15 A; A/B=171-650.
DR PDB; 6CD2; X-ray; 3.70 A; C=28-836.
DR PDB; 7LHG; EM; 3.80 A; C=28-836.
DR PDB; 7LHH; EM; 7.20 A; C=28-836.
DR PDB; 7LHI; EM; 7.60 A; C=28-836.
DR PDBsum; 2KT6; -.
DR PDBsum; 2VQI; -.
DR PDBsum; 3FIP; -.
DR PDBsum; 6CD2; -.
DR PDBsum; 7LHG; -.
DR PDBsum; 7LHH; -.
DR PDBsum; 7LHI; -.
DR AlphaFoldDB; P07110; -.
DR SMR; P07110; -.
DR DIP; DIP-60749N; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 1.B.11.2.1; the outer membrane fimbrial usher porin (fup) family.
DR EvolutionaryTrace; P07110; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015473; F:fimbrial usher porin activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009297; P:pilus assembly; IEA:InterPro.
DR Gene3D; 2.60.40.2070; -; 1.
DR Gene3D; 2.60.40.2610; -; 1.
DR Gene3D; 3.10.20.410; -; 1.
DR InterPro; IPR000015; Fimb_usher.
DR InterPro; IPR018030; Fimbrial_membr_usher_CS.
DR InterPro; IPR042186; FimD_plug_dom.
DR InterPro; IPR025949; PapC-like_C.
DR InterPro; IPR043142; PapC-like_C_sf.
DR InterPro; IPR025885; PapC_N.
DR InterPro; IPR037224; PapC_N_sf.
DR PANTHER; PTHR30451; PTHR30451; 1.
DR Pfam; PF13953; PapC_C; 1.
DR Pfam; PF13954; PapC_N; 1.
DR Pfam; PF00577; Usher; 1.
DR SUPFAM; SSF141729; SSF141729; 1.
DR PROSITE; PS01151; FIMBRIAL_USHER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Fimbrium biogenesis;
KW Membrane; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..24
FT CHAIN 25..836
FT /note="Outer membrane usher protein PapC"
FT /id="PRO_0000009323"
FT DISULFID 814..832
FT /evidence="ECO:0000255"
FT CONFLICT 517..543
FT /note="YSRQTYWDIRKTDYYTVSVNRYFNVFG -> SENIKVAVDAHRIIVRFPYVP
FT VCLTAV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 174..185
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 192..203
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 234..244
FT /evidence="ECO:0007829|PDB:3FIP"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 383..392
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 395..406
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 425..436
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 442..452
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:3FIP"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 494..505
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 512..525
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 528..537
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 548..554
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 565..572
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 590..599
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 606..615
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 622..632
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 634..645
FT /evidence="ECO:0007829|PDB:3FIP"
FT STRAND 758..764
FT /evidence="ECO:0007829|PDB:2KT6"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:2KT6"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:2KT6"
FT STRAND 792..796
FT /evidence="ECO:0007829|PDB:2KT6"
FT STRAND 806..810
FT /evidence="ECO:0007829|PDB:2KT6"
FT STRAND 814..818
FT /evidence="ECO:0007829|PDB:2KT6"
FT STRAND 824..834
FT /evidence="ECO:0007829|PDB:2KT6"
SQ SEQUENCE 836 AA; 91509 MW; 9343D35DC7B1E4C8 CRC64;
MKDRIPFAVN NITCVILLSL FCNAASAVEF NTDVLDAADK KNIDFTRFSE AGYVLPGQYL
LDVIVNGQSI SPASLQISFV EPALSGDKAE KKLPQACLTS DMVRLMGLTA ESLDKVVYWH
DGQCADFHGL PGVDIRPDTG AGVLRINMPQ AWLEYSDATW LPPSRWDDGI PGLMLDYNLN
GTVSRNYQGG DSHQFSYNGT VGGNLGPWRL RADYQGSQEQ SRYNGEKTTN RNFTWSRFYL
FRAIPRWRAN LTLGENNINS DIFRSWSYTG ASLESDDRML PPRLRGYAPQ ITGIAETNAR
VVVSQQGRVL YDSMVPAGPF SIQDLDSSVR GRLDVEVIEQ NGRKKTFQVD TASVPYLTRP
GQVRYKLVSG RSRGYGHETE GPVFATGEAS WGLSNQWSLY GGAVLAGDYN ALAAGAGWDL
GVPGTLSADI TQSVARIEGE RTFQGKSWRL SYSKRFDNAD ADITFAGYRF SERNYMTMEQ
YLNARYRNDY SSREKEMYTV TLNKNVADWN TSFNLQYSRQ TYWDIRKTDY YTVSVNRYFN
VFGLQGVAVG LSASRSKYLG RDNDSAYLRI SVPLGTGTAS YSGSMSNDRY VNMAGYTDTF
NDGLDSYSLN AGLNSGGGLT SQRQINAYYS HRSPLANLSA NIASLQKGYT SFGVSASGGA
TITGKGAALH AGGMSGGTRL LVDTDGVGGV PVDGGQVVTN RWGTGVVTDI SSYYRNTTSV
DLKRLPDDVE ATRSVVESAL TEGAIGYRKF SVLKGKRLFA ILRLADGSQP PFGASVTSEK
GRELGMVADE GLAWLSGVTP GETLSVNWDG KIQCQVNVPE TAISDQQLLL PCTPQK
