ID Q6HPC1_BACHK Unreviewed; 243 AA.
AC Q6HPC1;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Protein disulfide isomerase (S-S rearrangase) {ECO:0000313|EMBL:AAT58962.1};
DE EC=5.3.4.1 {ECO:0000313|EMBL:AAT58962.1};
GN Name=frnE {ECO:0000313|EMBL:AAT58962.1};
GN OrderedLocusNames=BT9727_0246 {ECO:0000313|EMBL:AAT58962.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT58962.1, ECO:0000313|Proteomes:UP000001301};
RN [1] {ECO:0000313|EMBL:AAT58962.1, ECO:0000313|Proteomes:UP000001301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27 {ECO:0000313|EMBL:AAT58962.1,
RC ECO:0000313|Proteomes:UP000001301};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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DR EMBL; AE017355; AAT58962.1; -; Genomic_DNA.
DR RefSeq; WP_000687920.1; NC_005957.1.
DR RefSeq; YP_034599.1; NC_005957.1.
DR AlphaFoldDB; Q6HPC1; -.
DR KEGG; btk:BT9727_0246; -.
DR PATRIC; fig|281309.8.peg.262; -.
DR HOGENOM; CLU_069253_0_2_9; -.
DR Proteomes; UP000001301; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd03024; DsbA_FrnE; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR PANTHER; PTHR13887:SF41; THIOREDOXIN SUPERFAMILY PROTEIN; 1.
DR Pfam; PF01323; DSBA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:AAT58962.1}.
FT DOMAIN 3..206
FT /note="DSBA-like thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF01323"
FT REGION 215..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 27174 MW; DE976AC4AACA9E76 CRC64;
MKIEVWSDFV CPFCYIGKRR LEMALEQFPH KKDVEVEFKS FELDPNAPIY SGTSINEVLA
SKYGISIEEA KRNNVQLGNH AASMGLSFNF DEMKPTNTFD AHRLAKFAKN QGKEKEITEN
LLFAYFTESK NLSDVDTLAT IAEASGLDKQ EALKVINDKS AYANDVRVDE AIAQQYQISG
VPYFIINQKY AISGAQPLET FVGALQQVWE EENPVPKLQE LSSEGGSDMS CTDKSCSVPS
KEQ
//
