DSBB_XYLFA
ID DSBB_XYLFA Reviewed; 173 AA.
AC Q9PGG2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Disulfide bond formation protein B {ECO:0000255|HAMAP-Rule:MF_00286};
DE AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00286};
GN Name=dsbB {ECO:0000255|HAMAP-Rule:MF_00286}; OrderedLocusNames=XF_0340;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by oxidizing the DsbA protein. {ECO:0000255|HAMAP-
CC Rule:MF_00286}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00286}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00286}.
CC -!- SIMILARITY: Belongs to the DsbB family. {ECO:0000255|HAMAP-
CC Rule:MF_00286}.
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DR EMBL; AE003849; AAF83150.1; -; Genomic_DNA.
DR PIR; G82818; G82818.
DR RefSeq; WP_010892873.1; NC_002488.3.
DR AlphaFoldDB; Q9PGG2; -.
DR SMR; Q9PGG2; -.
DR STRING; 160492.XF_0340; -.
DR EnsemblBacteria; AAF83150; AAF83150; XF_0340.
DR KEGG; xfa:XF_0340; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_098660_1_1_6; -.
DR OMA; GGALYMQ; -.
DR Proteomes; UP000000812; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00286; DsbB; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR022920; Disulphide_bond_form_DsbB.
DR InterPro; IPR023380; DsbB-like_sf.
DR Pfam; PF02600; DsbB; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW Electron transport; Membrane; Oxidoreductase; Redox-active center;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..173
FT /note="Disulfide bond formation protein B"
FT /id="PRO_0000059367"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 29..46
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 47..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 64..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 89..145
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT TOPO_DOM 165..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT DISULFID 38..41
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
FT DISULFID 104..131
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00286"
SQ SEQUENCE 173 AA; 19231 MW; 626DF05E3FB3A49C CRC64;
MNALQWSFRA QCLTGFLFCT GLLAYAIFLQ LHQGLEPCPL CIFQRIAFAV LGILFLIAGL
YNSSNVYTRK AYGLLIFLTA AIGTGIAGRH VWVQLMPHNT ISSCGSPLSF LSETMGPFEV
FRTVLTGTSD CGNIDWRFLG LSMPMWSMFW FVALALLGLL VGFKAERRKP LFS
