CDIB_ECOLX
ID CDIB_ECOLX Reviewed; 588 AA.
AC Q3YL97;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Outer membrane transporter CdiB {ECO:0000305};
GN Name=cdiB {ECO:0000303|PubMed:16109881};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000312|EMBL:AAZ57197.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=EC93;
RX PubMed=16109881; DOI=10.1126/science.1115109;
RA Aoki S.K., Pamma R., Hernday A.D., Bickham J.E., Braaten B.A., Low D.A.;
RT "Contact-dependent inhibition of growth in Escherichia coli.";
RL Science 309:1245-1248(2005).
RN [2]
RP FUNCTION.
RC STRAIN=EC93;
RX PubMed=19124575; DOI=10.1128/jb.01437-08;
RA Aoki S.K., Webb J.S., Braaten B.A., Low D.A.;
RT "Contact-dependent growth inhibition causes reversible metabolic
RT downregulation in Escherichia coli.";
RL J. Bacteriol. 191:1777-1786(2009).
RN [3]
RP FUNCTION.
RC STRAIN=EC93;
RX PubMed=21085179; DOI=10.1038/nature09490;
RA Aoki S.K., Diner E.J., de Roodenbeke C.T., Burgess B.R., Poole S.J.,
RA Braaten B.A., Jones A.M., Webb J.S., Hayes C.S., Cotter P.A., Low D.A.;
RT "A widespread family of polymorphic contact-dependent toxin delivery
RT systems in bacteria.";
RL Nature 468:439-442(2010).
CC -!- FUNCTION: Potential outer membrane protein component of a toxin-
CC immunity protein module, which functions as a cellular contact-
CC dependent growth inhibition (CDI) system. CDI modules allow bacteria to
CC communicate with and inhibit the growth of closely related neighboring
CC bacteria in a contact-dependent fashion. This protein may be required
CC for secretion and assembly of the CdiA toxin protein. Inhibitory cells
CC must be in logarithmic (not stationary) phase to inhibit growth of
CC their targets, while the presence of P or S but not type 1 pili
CC protects the target cells against growth inhibition.
CC {ECO:0000269|PubMed:16109881, ECO:0000305|PubMed:19124575,
CC ECO:0000305|PubMed:21085179}.
CC -!- FUNCTION: Probable member of a two partner secretion pathway (TPS) in
CC which it mediates the secretion of CdiA. {ECO:0000305|PubMed:16109881}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:16109881}.
CC -!- DISRUPTION PHENOTYPE: Loss of contact-dependent growth inhibition.
CC {ECO:0000269|PubMed:16109881}.
CC -!- SIMILARITY: Belongs to the TPS (TC 1.B.20) family. {ECO:0000305}.
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DR EMBL; DQ100454; AAZ57197.1; -; Genomic_DNA.
DR PDB; 6WIM; X-ray; 2.60 A; A=53-588.
DR PDBsum; 6WIM; -.
DR AlphaFoldDB; Q3YL97; -.
DR SMR; Q3YL97; -.
DR TCDB; 1.B.20.1.3; the two-partner secretion (tps) family.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR005565; Hemolysn_activator_HlyB_C.
DR InterPro; IPR013686; Polypept-transport_assoc_ShlB.
DR InterPro; IPR034746; POTRA.
DR InterPro; IPR035251; ShlB_POTRA.
DR InterPro; IPR027282; TPS.
DR Pfam; PF08479; POTRA_2; 1.
DR Pfam; PF17287; POTRA_3; 1.
DR Pfam; PF03865; ShlB; 1.
DR PIRSF; PIRSF029745; FhaC; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Membrane; Porin;
KW Protein transport; Transmembrane; Transmembrane beta strand; Transport.
FT CHAIN 1..588
FT /note="Outer membrane transporter CdiB"
FT /id="PRO_0000432084"
FT DOMAIN 104..179
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT HELIX 57..82
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:6WIM"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 300..315
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 318..333
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 340..360
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 363..380
FT /evidence="ECO:0007829|PDB:6WIM"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 390..405
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 408..419
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 441..467
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 495..512
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 518..531
FT /evidence="ECO:0007829|PDB:6WIM"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 540..554
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 557..568
FT /evidence="ECO:0007829|PDB:6WIM"
FT STRAND 579..587
FT /evidence="ECO:0007829|PDB:6WIM"
SQ SEQUENCE 588 AA; 64522 MW; C8C60FFB72B190B6 CRC64;
MRHRQDNLLA NRTLLPGMAS GQYVFRLCTF SPVVRYFSLL PCLCILSFSS PAAMLSPGDR
SAIQQQQQQL LDENQRQRDA LERSAPLTIT PSPETSAGTE GPCFTVSSIV VSGATRLTSA
ETDRLVAPWV NQCLNITGLT AVTDAMTDSY IRRGYITSRA FLTEQDLSGG VLHITVMEGR
LQQIRAEGAD LPARTLKMVF PGMEGKVLNL RDIEQGMEQI NRLRTEPVQI EISPGDREGW
SVVTLTALPE WPVTGSVGID NSGQKSTGTG QLNGVLSFNN PLGLADNWFV SGGRSSDFSV
SHDARNFAAG VSLPYGYTLV DYTYSWSDYL STIDNRGWRW RSTGDLQTHR LGLSHVLFRN
GDMKTALTGG LQHRIIHNYL DDVLLQGSSR KLTSFSVGLN HTHKFLGGVG TLNPVFTRGM
PWFGAESDHG KRGDLPVNQF RKWSVSASFQ RPVTDRVWWL TSAYAQWSPD RLHGVEQLSL
GGESSVRGFK DQYISGNNGG YLRNELSWSL FSLPYVGTVR AVAALDGGWL HSDSDDPYSS
GTLWGAAAGL STTSGHVSGS FTAGLPLVYP DWLAPDHLTV YWRVAVAF
