ID C3M8C4_HAMD5 Unreviewed; 310 AA.
AC C3M8C4;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=trbB {ECO:0000313|EMBL:ACQ68895.1};
GN OrderedLocusNames=HDEF_p0018 {ECO:0000313|EMBL:ACQ68895.1};
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OG Plasmid pHD5AT {ECO:0000313|EMBL:ACQ68895.1,
OG ECO:0000313|Proteomes:UP000002334}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX NCBI_TaxID=572265 {ECO:0000313|EMBL:ACQ68895.1, ECO:0000313|Proteomes:UP000002334};
RN [1] {ECO:0000313|EMBL:ACQ68895.1, ECO:0000313|Proteomes:UP000002334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT {ECO:0000313|Proteomes:UP000002334};
RC PLASMID=pHD5AT {ECO:0000313|EMBL:ACQ68895.1,
RC ECO:0000313|Proteomes:UP000002334};
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|RuleBase:RU364038}.
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DR EMBL; CP001278; ACQ68895.1; -; Genomic_DNA.
DR AlphaFoldDB; C3M8C4; -.
DR KEGG; hde:HDEF_p0018; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_057292_0_0_6; -.
DR Proteomes; UP000002334; Plasmid pHD5AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Periplasm {ECO:0000256|RuleBase:RU364038};
KW Plasmid {ECO:0000313|EMBL:ACQ68895.1};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|RuleBase:RU364038};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 174..283
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 310 AA; 34348 MW; 5F0ADADD9F9E0FDF CRC64;
MHSKPFFTHL IGNLMTTRID DADRGSVLFT CSLGKEPHFF IRQNSLIFRQ KHQKDLVLFS
DSESPDKAQH LLNALTEALV RRQKTKLFWR NLFFGLGFLA LLAIGSHGLL SETHTTDDIP
LARADSASAP LLPEENAIEK GLMQEPSPAL TTLAHNLRDA AQRKIFTVPL TTGHSRTIYV
FSDPLCPHCR DLEPTLEAIG KKVNIDLFPV SLIGKKATAD QVIPVLCASP EHRKALWHSL
FDDPPLTPSA SCDIGEKALA VNNKAFSAYG FRGTPQLISD DGRPIPLSAL KNEDTFSSFM
NAEPQEKKDE
//
