ID S3NNF2_9GAMM Unreviewed; 270 AA.
AC S3NNF2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=F945_00264 {ECO:0000313|EMBL:EPF81630.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF81630.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF81630.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF81630.1,
RC ECO:0000313|Proteomes:UP000014568};
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 Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-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:EPF81630.1}.
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DR EMBL; ATGI01000002; EPF81630.1; -; Genomic_DNA.
DR RefSeq; WP_016654714.1; NZ_KE340348.1.
DR AlphaFoldDB; S3NNF2; -.
DR STRING; 632955.GCA_000829675_00835; -.
DR PATRIC; fig|421052.3.peg.264; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_0_0_6; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000014568; 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 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.
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:UP000014568};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 23..270
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010009449"
FT DOMAIN 68..115
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 147..268
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 270 AA; 29915 MW; 1A1494BB0CFB2D78 CRC64;
MLLNRSRIFI ACALASTLIL SACSKSTESK KDDTLTATTP ATAEASNITE RNTQKRLINT
LEGHFKMANI NAKIKEIKPT EVPNLYWVNL EGMSAVYATS DGKFLIQGDV LRLGDKEITN
ISDKIQAAEN KKIFAALKVE DLIVYPAKGK AKHVVYIFTD ASCPYCHKLH SHIPEMNSKG
IEVRYIAWPR GEQFMPVMES VWCSANRQEA FEKAVAGEAL PPAQCKNPVS DQYQMGLNMG
VNGTPAIYNT EGEHIGAYMT ADELLKRLDK
//
