ID A0A3S5ABK6_9NEIS Unreviewed; 233 AA.
AC A0A3S5ABK6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thiol:disulfide interchange protein DsbA {ECO:0000256|ARBA:ARBA00013831};
GN Name=dsbA {ECO:0000313|EMBL:VEJ51713.1};
GN ORFNames=NCTC12742_01613 {ECO:0000313|EMBL:VEJ51713.1};
OS Neisseria weaveri.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=28091 {ECO:0000313|EMBL:VEJ51713.1, ECO:0000313|Proteomes:UP000272771};
RN [1] {ECO:0000313|EMBL:VEJ51713.1, ECO:0000313|Proteomes:UP000272771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12742 {ECO:0000313|EMBL:VEJ51713.1,
RC ECO:0000313|Proteomes:UP000272771};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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DR EMBL; LR134533; VEJ51713.1; -; Genomic_DNA.
DR RefSeq; WP_004283519.1; NZ_POXU01000002.1.
DR AlphaFoldDB; A0A3S5ABK6; -.
DR STRING; 28091.SAMEA3174300_00172; -.
DR KEGG; nwe:SAMEA3174300_0172; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000272771; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd03019; DsbA_DsbA; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR023205; DsbA/DsbL.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:VEJ51713.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000272771};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..233
FT /note="Thiol:disulfide interchange protein DsbA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018618520"
FT DOMAIN 10..208
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 233 AA; 25542 MW; A8D725171F1ABC88 CRC64;
MKLKTLLLGT LAALTVTAQA HAAVVEGKDY TVLDKPVPQL QSDKVEVLEF FGYFCVHCYH
LDPILLKHAQ SFADDTYLRT EHVVWEPAML GFARVAAAVN SSGLKYQANP EVFKAVYDQK
INLADTATFK EWAEKQSSFD GKKLVAAYDS FGNMAQAKKM EELTNAYQIS GTPTVIVGGK
YQVKFSGDWQ SGMKTIDELV AKVREEKGLK SAAAKPAAVL KSKGAWLAKS ANK
//
