ID   NRFX_HAEIN              Reviewed;         176 AA.
AC   P44943;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable thiol:disulfide interchange protein DsbE-2;
DE   AltName: Full=Cytochrome c biogenesis protein NrfX;
GN   Name=nrfX; Synonyms=dsbE-2; OrderedLocusNames=HI_0935;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Could be involved in disulfide bond formation. Could
CC       catalyzes a late, reductive step in the assembly of periplasmic NrfA c-
CC       type cytochrome, probably the reduction of disulfide bonds of the
CC       apocytochrome c to allow covalent linkage with the heme. Possible
CC       subunit of a heme lyase.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22593.1; -; Genomic_DNA.
DR   PIR; I64161; I64161.
DR   RefSeq; NP_439095.1; NC_000907.1.
DR   RefSeq; WP_005693282.1; NC_000907.1.
DR   AlphaFoldDB; P44943; -.
DR   SMR; P44943; -.
DR   STRING; 71421.HI_0935; -.
DR   PRIDE; P44943; -.
DR   EnsemblBacteria; AAC22593; AAC22593; HI_0935.
DR   KEGG; hin:HI_0935; -.
DR   PATRIC; fig|71421.8.peg.976; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_19_1_6; -.
DR   OMA; CKEEHPL; -.
DR   PhylomeDB; P44943; -.
DR   BioCyc; HINF71421:G1GJ1-975-MON; -.
DR   Proteomes; UP000000579; 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW   Disulfide bond; Membrane; Redox-active center; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..176
FT                   /note="Probable thiol:disulfide interchange protein DsbE-2"
FT                   /id="PRO_0000201307"
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..176
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        75..78
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   176 AA;  19926 MW;  078B408F97A8E48B CRC64;
     MNKKLIFFTP LFVLLGVCIL LIAGLNQDPK KIASALIDKP VPEFYQANLH EPSQIVSPKE
     FPKQPFLLNV WGSWCGYCKE EHPLLIEIAK TLPIVGVDYR DNRQNGIKML KRMGNPFILT
     IDDSHGELGL KLGVDGAPET YLVDENGVIR YRHSGLLDKE TWQTVFLPKI EALKNK