ID A0A0D5MA76_9GAMM Unreviewed; 251 AA.
AC A0A0D5MA76;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
DE Flags: Precursor;
GN ORFNames=KO116_P200013 {ECO:0000313|EMBL:AJY53120.1};
OS Halomonas sp. KO116.
OG Plasmid unnamed2 {ECO:0000313|EMBL:AJY53120.1,
OG ECO:0000313|Proteomes:UP000028645}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY53120.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY53120.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY53120.1,
RC ECO:0000313|Proteomes:UP000028645};
RC PLASMID=Plasmid unnamed2 {ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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; CP011054; AJY53120.1; -; Genomic_DNA.
DR RefSeq; WP_052703870.1; NZ_CP011054.1.
DR AlphaFoldDB; A0A0D5MA76; -.
DR KEGG; hak:KO116_P200013; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_095613_0_0_6; -.
DR OrthoDB; 9780340at2; -.
DR Proteomes; UP000028645; Plasmid unnamed2.
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:AJY53120.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Plasmid {ECO:0000313|EMBL:AJY53120.1};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 23..251
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010003974"
FT DOMAIN 48..90
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 127..235
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 251 AA; 27454 MW; 15AC8A529193E8FE CRC64;
MKTLLHTAVL VASMATAITA NASLTPASPI ADSPLFASIP FEELTLEHMD IRQIIPMPIN
GLSAIDNAGQ VMYASSNGRF VFIGQMYDLW KGGALETMEE IEQASTRIYL DGLQLHPRDL
NTVTIGNGPI DITIFTDPLC EHCHALAHEA KAYSDDYTFY FVVVPALGDE SHELAQRLHC
AENPSEGAEA LLNGTINLLA TRENCDLEGY EKTLLASEVL GVNGVPFLIH QDGRVNRGRP
QHLDQWLQGG R
//
