ID N9QF04_9GAMM Unreviewed; 271 AA.
AC N9QF04;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=F887_00299 {ECO:0000313|EMBL:ENX44373.1};
OS Acinetobacter sp. NIPH 2100.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217708 {ECO:0000313|EMBL:ENX44373.1, ECO:0000313|Proteomes:UP000013196};
RN [1] {ECO:0000313|EMBL:ENX44373.1, ECO:0000313|Proteomes:UP000013196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2100 {ECO:0000313|EMBL:ENX44373.1,
RC ECO:0000313|Proteomes:UP000013196};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2100.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:ENX44373.1}.
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DR EMBL; APSB01000001; ENX44373.1; -; Genomic_DNA.
DR RefSeq; WP_005154739.1; NZ_KB850224.1.
DR AlphaFoldDB; N9QF04; -.
DR STRING; 1217708.F887_00299; -.
DR PATRIC; fig|1217708.3.peg.289; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_0_0_6; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000013196; 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; IPR013766; Thioredoxin_domain.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 23..271
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010008572"
FT DOMAIN 133..271
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 271 AA; 29833 MW; ABF01828C11902D3 CRC64;
MLFTRSQLVI ACTLASTLLV SACSKENSAQ KQDALTASAP ATGEASTLNE RNTQQRLVST
LEKHFKTANI NAKILVIKKT EVPNLYWVSL EGMGSVYATA DGQYIIQGDV VRLGDKQLHN
VSEALQATEN KKHLASLKTE DLIVYPAQGG KAKHVIYVFT DSSCPYCHKL HEHLAEINAK
GIEVRYIAWP RGEQFMPTMQ AIWCSQDRKA AFDQAAKGLP VSAAECKNPV RDQYQLGLNM
GVNGTPAIYN VEGEYLGGYM TPEEIAQRLN K
//
