ID A0A1B2M493_9GAMM Unreviewed; 679 AA.
AC A0A1B2M493;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:AOA59961.1};
GN ORFNames=BFG52_10165 {ECO:0000313|EMBL:AOA59961.1};
OS Acinetobacter larvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1789224 {ECO:0000313|EMBL:AOA59961.1, ECO:0000313|Proteomes:UP000093391};
RN [1] {ECO:0000313|EMBL:AOA59961.1, ECO:0000313|Proteomes:UP000093391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRTC-1 {ECO:0000313|EMBL:AOA59961.1,
RC ECO:0000313|Proteomes:UP000093391};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP016895; AOA59961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B2M493; -.
DR STRING; 1789224.BFG52_10165; -.
DR KEGG; ala:BFG52_10165; -.
DR Proteomes; UP000093391; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF11412; DsbD_N; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000093391};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 273..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 550..675
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 679 AA; 76521 MW; AF935AF44CFBA24B CRC64;
MALLLSNILT THTAYAESKF LPPQQAFQFS AESVSPQQIK LQWKIADHYY LYHDQFKVKQ
QQQAIKLQLP AGQAKNDPTF GLTDVHYGQV QATIQVQPEK RYTIFWQGCA EEGLCYPMQR
ATFQTDSTGL LISEQNTTQH NALLPPPKVT NQAHRLNLDT FETAASKQNH AQSVDQKTAD
KFIPTKEQGR PAIKSEKLEV ASSLTTDIAP ETNEVDQINT DVTHTPEQKN IAQITETTVD
PTENHKLIST PKESTFSLNN DQQFLQLLSP DRFLINLGVF FILGILLAFL PCSLPLIPIL
SGIIVQRSQG YKAVAVALCF VVSMALVYSL MGIIVAEIGY SVQRWFQNPW IIGSFAVIFI
LLAFNLFGLY QLSLPQVFIN KLDQLQNKQQ GGTFIGAAIM GALSALIVGP CMSAPLAGAL
LFVSQSQNAL MGGLYLFILG LGLGLPLFIA SVFGAKYLPK PGDWMDRLKF CFGFMMLILA
VYFIRPMIGS FYYAVLLAVL CIALSVYFIY LIRVSHKVWT RLFFIAAIGC SIWAAVWQSQ
QAYYAKQHHL QREHLLPWQQ VNTTEQLQQA LQQARQEQRP ILIDVYADWC VACQPIENDV
MPHPDVQQQL QRLVRIKLDL THYHPSQEQI LQQHEILGPP TMLFLNPEGQ EQRELRLTGS
FSASKFIQQM QRLQATQAQ
//
