(data stored in ACNUC7421 zone)

SWISSPROT: DSBB2_PSEU2

ID   DSBB2_PSEU2             Reviewed;         175 AA.
AC   Q500P0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Disulfide bond formation protein B 2 {ECO:0000255|HAMAP-Rule:MF_00286};
DE   AltName: Full=Disulfide oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_00286};
GN   Name=dsbB2 {ECO:0000255|HAMAP-Rule:MF_00286};
GN   OrderedLocusNames=Psyr_0058;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by oxidizing the DsbA protein.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000075; AAY35132.1; -; Genomic_DNA.
DR   RefSeq; WP_003401558.1; NC_007005.1.
DR   RefSeq; YP_233170.1; NC_007005.1.
DR   STRING; 205918.Psyr_0058; -.
DR   EnsemblBacteria; AAY35132; AAY35132; Psyr_0058.
DR   GeneID; 3365533; -.
DR   KEGG; psb:Psyr_0058; -.
DR   PATRIC; fig|205918.7.peg.57; -.
DR   eggNOG; COG1495; LUCA.
DR   HOGENOM; HOG000218136; -.
DR   KO; K03611; -.
DR   OMA; TLPEWSL; -.
DR   BioCyc; PSYR205918:G1G4J-58-MONOMER; -.
DR   Proteomes; UP000000426; 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 oxidoreductase activity; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; Q500P0.
DR   SWISS-2DPAGE; Q500P0.
KW   Cell inner membrane; Cell membrane; Chaperone; Complete proteome;
KW   Disulfide bond; Electron transport; Membrane; Oxidoreductase;
KW   Redox-active center; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    175       Disulfide bond formation protein B 2.
FT                                /FTId=PRO_0000298395.
FT   TOPO_DOM      1      9       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TRANSMEM     10     26       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TOPO_DOM     27     44       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TRANSMEM     45     61       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TOPO_DOM     62     68       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TRANSMEM     69     85       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TOPO_DOM     86    142       Periplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TRANSMEM    143    161       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   TOPO_DOM    162    175       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
FT   DISULFID     36     39       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00286}.
SQ   SEQUENCE   175 AA;  18980 MW;  987935E364058676 CRC64;
     MYLARTRFLF FLASLACASI IGVAFYLQQA VGLDPCTLCM VQRAAFIACG VLALCAACHA
     PGPTGTRRYS LGLLLVALAG LAGAGTQVWL QTASADQLIP FITRLEQILS LLSLDMCIDR
     LRSDALFCAE ITWTLFGISL PEWSLLAFTG LALLPLYPLF SELSHWLATR DRGGY
//

If you have problems or comments...

PBIL Back to PBIL home page