ID U7P2X9_9GAMM Unreviewed; 245 AA.
AC U7P2X9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=Q671_05785 {ECO:0000313|EMBL:ERS89913.1};
OS Halomonas sp. PBN3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS89913.1, ECO:0000313|Proteomes:UP000017115};
RN [1] {ECO:0000313|EMBL:ERS89913.1, ECO:0000313|Proteomes:UP000017115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBN3 {ECO:0000313|EMBL:ERS89913.1,
RC ECO:0000313|Proteomes:UP000017115};
RX PubMed=24356826;
RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA Kostka J.E.;
RT "Draft genome sequences for oil-degrading bacterial strains from beach
RT sands impacted by the deepwater horizon oil spill.";
RL Genome Announc. 1:e01015-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERS89913.1}.
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DR EMBL; AXCA01000149; ERS89913.1; -; Genomic_DNA.
DR RefSeq; WP_023005504.1; NZ_AXCA01000149.1.
DR AlphaFoldDB; U7P2X9; -.
DR PATRIC; fig|1397528.3.peg.1302; -.
DR eggNOG; COG1651; Bacteria.
DR Proteomes; UP000017115; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 InterPro; IPR017937; Thioredoxin_CS.
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.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364038};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 24..245
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010005504"
FT DOMAIN 36..82
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 123..241
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 245 AA; 26495 MW; AF4459DE0508872E CRC64;
MTTLSRTLLA TLLAAPLALP ALAEQDGAER LAERLAVNGQ AMPVQSVREA PMEGLFEVRL
ATGERFYSDA EGEHFLVGDL YRNAEQGLVN LTEQARNGER AARLAEVPEA ERVIFRGPES
EAEVVVFTDT TCPYCQQLHE EVPRLNELGI EVHYLAFPRS GMNGQGAREL QQVWCAENPA
EAMSAAKRDD SLSGAADCDN PVEAQYHLGL ELGVQGTPAI VLPDGRLVPG YVPAERLAAM
LGVAE
//