ID   TXLA_SYNE7              Reviewed;         191 AA.
AC   P35088; Q31LB1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Thiol:disulfide interchange protein TxlA;
GN   Name=txlA; OrderedLocusNames=Synpcc7942_2128;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7768827; DOI=10.1128/jb.177.11.3269-3276.1995;
RA   Collier J.L., Grossman A.R.;
RT   "Disruption of a gene encoding a novel thioredoxin-like protein alters the
RT   cyanobacterial photosynthetic apparatus.";
RL   J. Bacteriol. 177:3269-3276(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins. Acts
CC       by transferring its disulfide bond to other proteins and is reduced in
CC       the process.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; U05044; AAA89104.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58158.1; -; Genomic_DNA.
DR   PIR; A57254; A57254.
DR   RefSeq; WP_011244274.1; NC_007604.1.
DR   AlphaFoldDB; P35088; -.
DR   SMR; P35088; -.
DR   STRING; 1140.Synpcc7942_2128; -.
DR   PRIDE; P35088; -.
DR   EnsemblBacteria; ABB58158; ABB58158; Synpcc7942_2128.
DR   KEGG; syf:Synpcc7942_2128; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_064833_2_0_3; -.
DR   OMA; DNTKWLP; -.
DR   OrthoDB; 1630944at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2128-MON; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR044241; TxlA/HCF164.
DR   PANTHER; PTHR47353; PTHR47353; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Membrane; Redox-active center;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..191
FT                   /note="Thiol:disulfide interchange protein TxlA"
FT                   /id="PRO_0000120178"
FT   TRANSMEM        14..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..148
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          165..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        69..72
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   191 AA;  20661 MW;  8C88B397AD40F640 CRC64;
     MTADNSVPSR LRNILVIAAA LVLTILVVLG SRQPSAAASL ASLAEQATPY EVAIANDRPM
     LLEFYADWCT SCQAMAGRIA ALKQDYSDRL DFVMLNIDND KWLPEVLDYN VDGIPQFVYL
     NGQGQPQGIS IGELPRSVLA ANLDALVEAQ PLPYTNARGN LSEFSADLQP SRSSQTDPRS
     HSGQVQDGVL D