ID D8ITM9_HERSS Unreviewed; 255 AA.
AC D8ITM9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=dsbC {ECO:0000313|EMBL:ADJ65659.1};
GN OrderedLocusNames=Hsero_4189 {ECO:0000313|EMBL:ADJ65659.1};
OS Herbaspirillum seropedicae (strain SmR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ65659.1, ECO:0000313|Proteomes:UP000000329};
RN [1] {ECO:0000313|EMBL:ADJ65659.1, ECO:0000313|Proteomes:UP000000329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ65659.1,
RC ECO:0000313|Proteomes:UP000000329};
RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B.,
RA Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F.,
RA Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E.,
RA Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G.,
RA Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O.,
RA Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G.,
RA Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C.,
RA Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P.,
RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M.,
RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C.,
RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P.,
RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P.,
RA Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C.,
RA Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M.,
RA Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K.,
RA Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E.,
RA Weiss V.A., Yates M.A., Souza E.M.;
RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-
RT fixing, plant-growth promoting beta-Proteobacteria.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by transferring its disulfide bond to other proteins and
CC is reduced in the process. {ECO:0000256|RuleBase:RU364038}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
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DR EMBL; CP002039; ADJ65659.1; -; Genomic_DNA.
DR RefSeq; WP_013236116.1; NC_014323.1.
DR AlphaFoldDB; D8ITM9; -.
DR STRING; 757424.Hsero_4189; -.
DR KEGG; hse:Hsero_4189; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_1_1_4; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000000329; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:ADJ65659.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000000329};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 34..255
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010006688"
FT DOMAIN 47..99
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 128..251
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 255 AA; 27944 MW; 167743C33CB58A11 CRC64;
MKNFLTAGAS SLRHLSMAAL LLASTVVGVS AHAQAEAAES TEATIKKLIE PRLGKDAKVD
AVTKTPYAGL YEIQIDGDVI YTDAKAQYLF IGRVVDSQTY RDYTKEKIES LNQIPFSGLP
LDKAIKTVKG NGKRVIAIFE DPNCIYCKRL HKTLQEVDNI TYYTFQYNIL SPDSIVKSRN
IWCAPNPSRA WSEWMVNGKE APAAATSCNA PHEDVLALGQ KLKVTGTPTI FFTDGSRIPG
AVDAKSLEQK LSSLK
//
