ID A0A066UMU0_9GAMM Unreviewed; 323 AA.
AC A0A066UMU0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=MBO_03512 {ECO:0000313|EMBL:KDN25533.1};
OS Moraxella bovoculi 237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN25533.1, ECO:0000313|Proteomes:UP000035860};
RN [1] {ECO:0000313|EMBL:KDN25533.1, ECO:0000313|Proteomes:UP000035860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=237 {ECO:0000313|EMBL:KDN25533.1,
RC ECO:0000313|Proteomes:UP000035860};
RX PubMed=24970830;
RA Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA Reilly T.J.;
RT "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL Genome Announc. 2:e00612-14(2014).
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:KDN25533.1}.
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DR EMBL; AOMT01000011; KDN25533.1; -; Genomic_DNA.
DR RefSeq; WP_036363699.1; NZ_AOMT01000011.1.
DR AlphaFoldDB; A0A066UMU0; -.
DR eggNOG; COG1651; Bacteria.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000035860; 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; 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; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000035860};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 22..323
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010002079"
FT DOMAIN 194..320
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 323 AA; 35084 MW; 2588C676165D9B8C CRC64;
MKTLLKSLSL AVILSLGTAH ANINEAQIRA TLNGAGLSIP VESIQPSPIS SLLLLSLGQG
QEPLLITHDL NYVIQGNIEP NPSPKAATGN HPKAKAGTPI TNAHKADLLA NMTVLKNIDQ
QAAFYHTNVD GLLWGVSASG TPFLVSSDGR YFINGEISVI EDGLFAGLDT DFEYAKNRHA
LGQLDQETLA IYPAKGTERA VVYIATDINC PYCKIFHSKI NEFNNKGITI KAIGYPVYDE
SPEPMRQIWC ESDNTKRASL LSAAMRGIRI RATCQGDENN LTHNQLAAQS LAIFATPAIF
NDQGELFQGD FNGEEFLEFL NIK
//