ID   A0A0H5MFY3_YERIN        Unreviewed;       701 AA.
AC   A0A0H5MFY3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Putative metal resistance protein {ECO:0000313|EMBL:CRY55981.1};
DE            EC=1.8.1.8 {ECO:0000313|EMBL:CRY55981.1};
GN   Name=scsB {ECO:0000313|EMBL:CRY55981.1};
GN   ORFNames=ERS008476_02999 {ECO:0000313|EMBL:CRY55981.1};
OS   Yersinia intermedia.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=631 {ECO:0000313|EMBL:CRY55981.1, ECO:0000313|Proteomes:UP000043316};
RN   [1] {ECO:0000313|Proteomes:UP000043316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R148 {ECO:0000313|Proteomes:UP000043316};
RG   Pathogen Informatics;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CWJI01000009; CRY55981.1; -; Genomic_DNA.
DR   RefSeq; WP_053009940.1; NZ_CWJI01000009.1.
DR   AlphaFoldDB; A0A0H5MFY3; -.
DR   Proteomes; UP000043316; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   CDD; cd02953; DsbDgamma; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
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; PS00194; THIOREDOXIN_1; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:CRY55981.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..701
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005221485"
FT   TRANSMEM        280..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        364..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        446..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        507..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        535..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..146
FT                   /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11412"
FT   DOMAIN          288..497
FT                   /note="Cytochrome C biogenesis protein transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02683"
SQ   SEQUENCE   701 AA;  76278 MW;  3F3EFF2AA681A105 CRC64;
     MLNLFKTGLF CLLLLWMPTL WAADSGWLVS PQNDHAKVRL RTEPSAGGET RMLLSVQLEK
     GWKTYWRSPG EGGIAPTIVW TPPLEKVKWF WPVPQRFDVS GISTQGYHEQ VMLPIVISGP
     LPKTLSGTLT LSTCSNVCIL TDYPFSLDLT SPINAANQQQ FEHDFAQAMG QVPIANALTK
     QIQAGYGNGE VQIHAIREEG WQQPALFFDT LEDADLGKPI VSVQGKQLSV RVPATDGWGE
     GSADLQGKQL TMVITDGGVA QEASVMIGPA ITLPTSSTAF WSWILMALTG GLILNLMPCV
     LPVLAMKLGS ILHTEHQTRR QVRWQFLASS AGIITSFWLL ALLMTALRLG NHALGWGIQF
     QNPWFIGFMV LVTALFTANL FGLFEIQLSS SLNTRIAAPR IEKSGVRGMA GHFGQGALAT
     LLATPCSAPF LGTAVAFALA APLPALWGIF TALGVGMSLP WLAVAAWPKL ALCLPKPGRW
     MNHLRIAMGV LMLASSLWLL SLMASHIGLQ AVMVMTGVLL LALIFAIGWR YGARIATIVS
     LISVLLVGSL LLAGSLTANL WQKPLHDNVA WQPLTESAIK QALHENKRVF VDVTADWCVT
     CKVNKLHVLM RDDVQKALQE PDVVALRGDW TRPSASITQF LRERGSVAIP FNQIYGPQLN
     GPQLNGSQLN SSQQQQGVVL SPLLDREVLL KELAAAKGNQ K
//