DSBE_PSEAE
ID DSBE_PSEAE Reviewed; 180 AA.
AC Q9I3N1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thiol:disulfide interchange protein DsbE;
DE AltName: Full=Cytochrome c biogenesis protein CcmG;
GN Name=dsbE; Synonyms=ccmG; OrderedLocusNames=PA1481;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Involved in disulfide bond formation. Catalyzes a late,
CC reductive step in the assembly of periplasmic c-type cytochromes,
CC probably the reduction of disulfide bonds of the apocytochrome c to
CC allow covalent linkage with the heme. Possible subunit of a heme lyase
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04870.1; -; Genomic_DNA.
DR PIR; B83460; B83460.
DR RefSeq; NP_250172.1; NC_002516.2.
DR RefSeq; WP_003083138.1; NZ_QZGE01000005.1.
DR PDB; 3KH7; X-ray; 1.75 A; A=26-180.
DR PDB; 3KH9; X-ray; 2.20 A; A=26-180.
DR PDBsum; 3KH7; -.
DR PDBsum; 3KH9; -.
DR AlphaFoldDB; Q9I3N1; -.
DR SMR; Q9I3N1; -.
DR STRING; 287.DR97_542; -.
DR PaxDb; Q9I3N1; -.
DR PRIDE; Q9I3N1; -.
DR DNASU; 881065; -.
DR EnsemblBacteria; AAG04870; AAG04870; PA1481.
DR GeneID; 881065; -.
DR KEGG; pae:PA1481; -.
DR PATRIC; fig|208964.12.peg.1532; -.
DR PseudoCAP; PA1481; -.
DR HOGENOM; CLU_042529_19_1_6; -.
DR InParanoid; Q9I3N1; -.
DR OMA; MIGKPFP; -.
DR PhylomeDB; Q9I3N1; -.
DR BioCyc; PAER208964:G1FZ6-1507-MON; -.
DR EvolutionaryTrace; Q9I3N1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR CDD; cd03010; TlpA_like_DsbE; 1.
DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00385; dsbE; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cytochrome c-type biogenesis; Disulfide bond; Membrane;
KW Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..180
FT /note="Thiol:disulfide interchange protein DsbE"
FT /id="PRO_0000201298"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..180
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..175
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 74..77
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3KH7"
FT TURN 32..37
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3KH7"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3KH7"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3KH7"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3KH7"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3KH7"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3KH7"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:3KH7"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:3KH7"
SQ SEQUENCE 180 AA; 20122 MW; 6C85E368106673F5 CRC64;
MKRAILLLPL GIFLIVAVFL FRGLWLDPSE LPSALIGKPF PAFDLPSVQD PARRLTEADL
KGKPALVNVW GTWCPSCRVE HPELTRLAEQ GVVIYGINYK DDNAAAIKWL NELHNPYLLS
ISDADGTLGL DLGVYGAPET YLIDKQGIIR HKIVGVVDQK VWREQLAPLY QQLLDEPEAR
