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Database: UniProt
Entry: A0A066UMU0_9GAMM
LinkDB: A0A066UMU0_9GAMM
Original site: A0A066UMU0_9GAMM 
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
//
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