ID A0A1A3MSH4_MYCAS Unreviewed; 571 AA.
AC A0A1A3MSH4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:OBK12873.1};
GN ORFNames=A5636_10340 {ECO:0000313|EMBL:OBK12873.1};
OS Mycobacterium asiaticum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1790 {ECO:0000313|EMBL:OBK12873.1, ECO:0000313|Proteomes:UP000093629};
RN [1] {ECO:0000313|EMBL:OBK12873.1, ECO:0000313|Proteomes:UP000093629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245139.5 {ECO:0000313|EMBL:OBK12873.1,
RC ECO:0000313|Proteomes:UP000093629};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBK12873.1}.
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DR EMBL; LZLQ01000121; OBK12873.1; -; Genomic_DNA.
DR RefSeq; WP_065160119.1; NZ_LZLQ01000121.1.
DR AlphaFoldDB; A0A1A3MSH4; -.
DR OrthoDB; 9811352at2; -.
DR Proteomes; UP000093629; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd03012; TlpA_like_DipZ_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR041017; Thioredoxin_10.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852:SF13; PROTEIN DIPZ; 1.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF17991; Thioredoxin_10; 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 Reference proteome {ECO:0000313|Proteomes:UP000093629};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..420
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 571 AA; 60133 MW; 8FC429F579B60776 CRC64;
MWTLALIGFL GGLITGISPC ILPVLPVIFF SGANSAAPTQ SEGAVAVQTK PEASRPYRVI
GGLVLSFSVV TLLGSAMLSA LHLPQDVIRW VALIALVAIG VGLIFPRFEQ LIERPFARIP
RQQIITRGNG FGLGLALGVL YVPCAGPVLA AIVVAGATAQ IGVGTVVLTA TFACGAALPL
LFFALAGQRV AQRVSAFRRH QREIRIGAGI VTILLAVALV FNLPAALQRA LPDYTAPLQD
KVGGTEQIRQ QLGGGIDANA LLSTCTNGGP RLMNCGTAPD LRGITDWLNT PGGQPIALNA
LRGKVVLIDF WAYSCINCQR AIPHVVGWYQ AYHDSGLEVV GVHTPEYAFE KVPENVAKGA
ADLGIRYPVA LDNSFSTWTN YHNSYWPAEY LIDAGGTVRH LKFGEGDYDT TEQLIRQLLT
DANPGVKLPP PVGAPDLTPK SFTTAETYLA VGKAVNYGGG GGYDEGTATF SYPPSLSSDS
FALNGQWSLD YQGATAAGDN SGLKLNYHAK NIYAVVGGTG TLTVLRNGKP TVLPISGPPT
SHQIVGDAAQ SGGTIEVRPT KGLQLFSFTY G
//
