CDIB2_BURP2
ID CDIB2_BURP2 Reviewed; 584 AA.
AC P0DMJ8;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Outer membrane transporter CdiB-2;
DE Short=CdiB-2;
DE AltName: Full=CdiB-II;
DE Flags: Precursor;
GN Name=cdiB2; OrderedLocusNames=BP1026B_II2204;
OS Burkholderia pseudomallei (strain 1026b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=884204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1026b;
RX PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA Jacobs M.A.;
RT "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL PLoS ONE 7:E36507-E36507(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=1026b;
RX PubMed=22435733; DOI=10.1111/j.1365-2958.2012.08039.x;
RA Nikolakakis K., Amber S., Wilbur J.S., Diner E.J., Aoki S.K., Poole S.J.,
RA Tuanyok A., Keim P.S., Peacock S., Hayes C.S., Low D.A.;
RT "The toxin/immunity network of Burkholderia pseudomallei contact-dependent
RT growth inhibition (CDI) systems.";
RL Mol. Microbiol. 84:516-529(2012).
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.
CC {ECO:0000269|PubMed:22435733}.
CC -!- FUNCTION: Expression of this cdiAIB locus in B.thailandensis confers
CC protection against other bacteria carrying the locus; growth inhibition
CC requires cellular contact. {ECO:0000269|PubMed:22435733}.
CC -!- FUNCTION: Probable member of a two partner secretion pathway (TPS) in
CC which it mediates the secretion of CdiA2. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene from the locus expressed in
CC B.thailandensis abrogates growth inhibition.
CC {ECO:0000269|PubMed:22435733}.
CC -!- SIMILARITY: Belongs to the TPS (TC 1.B.20) family.
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DR EMBL; CP002834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_038742387.1; NZ_CP004380.1.
DR AlphaFoldDB; P0DMJ8; -.
DR SMR; P0DMJ8; -.
DR TCDB; 1.B.20.1.10; the two-partner secretion (tps) family.
DR Proteomes; UP000010087; Chromosome 2.
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 3: Inferred from homology;
KW Cell outer membrane; Ion transport; Membrane; Porin; Protein transport;
KW Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..584
FT /note="Outer membrane transporter CdiB-2"
FT /id="PRO_0000429696"
FT DOMAIN 98..171
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT REGION 24..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 63654 MW; 34F0370186BE07A3 CRC64;
MATRFAILPV TALITLTAQA QQAPTPNDQA AAARANAEQN QQAQQRRDAQ QRDATVQAPG
VRSDVPRPEA YPVLPTETPC FQIDRFALDV PDSLPAASKA QGASALPMDR FAFARDWLAH
YAGQCIGKQG VDLIVKGLSQ AILARGYITT RVLVPEQDLS TGALKLALIP GVIRHVRFED
EKLLGTWKTA FPTRDGDVLN LRDIEQGLEQ MKRVSSQDVS MRIAPGDMPG ESDVVLDVKR
GKPWTVVASI DNSGTRATGK LQGNVSLGID NPLGLNDIFN VGFNQDLEFG DKRFGSHGWN
AFYSIPWGYW TGTLSAYTST YFQPLAAVNQ TFVASGNMKT VDFRLNRVLT RSRNDVLGAQ
VRLTRRFGDS YIEGTTIPSS HQNATFLEFG LNDRHYFGSS QFDGSLAYRQ GLGWLGSTDS
MFAAEGGQTY RFKMVVLDAN LSTPFVIGTQ PFKYVTTFHG QYTGNTVSYL DSVTIGSRYT
VRGFDGETLL AGSRGFYWRN ELQVPVAQTG LSAYAGLDYG RVWGPEPVAL VGTQLAGAVI
GVKGSLMTRF GGYGYDLFAG TPVYKPSGFP TARVTVGFQL TAQF