ID A0A0P7BZP8_9BACT Unreviewed; 685 AA.
AC A0A0P7BZP8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=AFM12_10645 {ECO:0000313|EMBL:KPM47729.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM47729.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM47729.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM47729.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-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:KPM47729.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGTQ01000009; KPM47729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BZP8; -.
DR STRING; 1605367.AFM12_10645; -.
DR PATRIC; fig|1605367.3.peg.3518; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000050454; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IPR028250; DsbDN.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR PANTHER; PTHR32234; 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; 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:UP000050454};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..685
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006136374"
FT TRANSMEM 232..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 514..682
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 685 AA; 76378 MW; 2367AF6654A6CEB0 CRC64;
MSKSYKLIIL LLLISKVSLA QILQPTTWKF QPAKKEVKVG EIIELQFNAT IQKDWYLYSS
DFDPDLGPIV TEVSFIPNSS YKLVGGIVPV HPKKKYDDLW GGNITYFTGK GQFLQKVKIL
KPEAKVDGKI SFQSCTDVDG RCVNGKEDFS FNVKGIASSA AEMAKPGIEK SAVEEQKDAV
ASKDEIEEAD EDVVSKLPTM EEAINNEAVI SENDEVINSD LPVQKEEEVT SLWKFLLLAL
GAGFASIFMP CIYPIMPMTV SFFTKQENGK SKAFFYGLSI MAIFAVMGLV TMAFGAPFLN
FISTHWIPNL IFFIIFILFG ISLLGAFEIV LPHEAVNKID RMSDRGGIIG IFFMALTLVV
VSFSCTVPFV GSLLILSAQG EVLRPLYGML AFGLPFAAVF TSLAMFPQWL KNLPKSGGWL
NELKAVFGFL EFGLALKFLS NIDLAYHWNL IHRNIFILIW VVIAVLIGLY ILGFLRLPKD
NRVEKFSLAR IVYSVIFFAF AAYMVPGVAN KSLPLLSGIL PPMPTSEVSA TIKPLAHEKM
KALPHGLQGF KDYDDALAYS EEVGKPVLID FTGYACANCR KMEEFVWPKE EVLKRLSEDF
VIASLYVDDK ATLPVEKHYI SSYDNEKKTT VGGKNMDLEI TKFNNNAQPY YAVVDSEGNP
LLEPIGYSSE EEFVEFLDKG KNLFQ
//