ID A0A0W0YKI9_9GAMM Unreviewed; 385 AA.
AC A0A0W0YKI9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:KTD57402.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:KTD57402.1};
GN ORFNames=Lsha_2587 {ECO:0000313|EMBL:KTD57402.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD57402.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD57402.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD57402.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KTD57402.1}.
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DR EMBL; LNYW01000068; KTD57402.1; -; Genomic_DNA.
DR RefSeq; WP_018578092.1; NZ_LNYW01000068.1.
DR AlphaFoldDB; A0A0W0YKI9; -.
DR STRING; 1122169.Lsha_2587; -.
DR PATRIC; fig|1122169.6.peg.2987; -.
DR eggNOG; COG4232; Bacteria.
DR Proteomes; UP000054600; Unassembled WGS sequence.
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 InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 Oxidoreductase {ECO:0000313|EMBL:KTD57402.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..381
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 385 AA; 41593 MW; DB2A9033462A0FAC CRC64;
MNKLLSIILM ITAGVITEPL QANSLSLADP QAIGQLIGTH GAPVYLALFF GLGILLAFTP
CVLPMIPILS GIIVGQDNLT TGRSFRLSLS YVMGMAITYA VAGMLAGYLG STVQTLMQQP
WVIISFSLVF VLLGLSMFGL FEIRMPAWLQ PRMRQGQGGL IAAGLMGILS TLIVSPCVTA
PLIAVLTFIS QSGQTGLGGL LLFVMALGMG LPLLLVGAGY GRFLPKSGAW MIRIKQLFGI
IMLLLAVWMV ARVMPMHTPT PAGFTMVHSM QELQQELAHA KEKHQPVFVE FYAGWCSDCR
AMDAKVFNQP DIVQAMQGSV NLRVDISDKS PAVASIRQIY GILGVPAMRF YNSNGELIPD
LLSHNQLDKQ QMLGLLNQFA TRVAP
//
