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Database: UniProt
Entry: A0A178GKS7_9GAMM
LinkDB: A0A178GKS7_9GAMM
Original site: A0A178GKS7_9GAMM 
ID   A0A178GKS7_9GAMM        Unreviewed;       282 AA.
AC   A0A178GKS7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Redoxin {ECO:0000313|EMBL:OAL85921.1};
GN   ORFNames=AY605_14400 {ECO:0000313|EMBL:OAL85921.1};
OS   Acinetobacter sp. SFD.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1805635 {ECO:0000313|EMBL:OAL85921.1, ECO:0000313|Proteomes:UP000186186};
RN   [1] {ECO:0000313|EMBL:OAL85921.1, ECO:0000313|Proteomes:UP000186186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SFD {ECO:0000313|EMBL:OAL85921.1,
RC   ECO:0000313|Proteomes:UP000186186};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OAL85921.1}.
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DR   EMBL; LSZJ01000006; OAL85921.1; -; Genomic_DNA.
DR   RefSeq; WP_064095381.1; NZ_LSZJ01000006.1.
DR   AlphaFoldDB; A0A178GKS7; -.
DR   STRING; 1805635.AY605_14400; -.
DR   Proteomes; UP000186186; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   GO; GO:0008961; F:phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001640; Lgt.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF01790; LGT; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        58..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          138..280
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   282 AA;  31756 MW;  9ECC605320FD992E CRC64;
     MMISSDALHL GPLMLPWTLI IVATGLVLLS AVLFGLARKY SWSKQLLGQS QDLLWSSFLL
     GMLGARLVFI LLNAELYFAA PIDILKIQDK GFHLWGGVLL GALWYVIRNR QLQTRFKAIL
     LIIFVLWIGL GLAFKSSLKT EAAFPDLAFA GLEQERLGTD KVSLSQFIGQ PTVINLWASW
     CPPCHREMPV LAKAAQQHPQ VNFVMLNQGE EVETVNAYLK KHQFQFKHVL LDPYGELPQQ
     LNSFGLPTTL FFNAQGQLVE RHMGELSPAM LQQYLNRISN QP
//
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