ID L0IVY1_9MYCO Unreviewed; 560 AA.
AC L0IVY1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Cytochrome c biogenesis protein {ECO:0000313|EMBL:AGB22758.1};
DE Flags: Precursor;
GN ORFNames=Mycsm_02421 {ECO:0000313|EMBL:AGB22758.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB22758.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003078; AGB22758.1; -; Genomic_DNA.
DR RefSeq; WP_015306338.1; NC_019966.1.
DR AlphaFoldDB; L0IVY1; -.
DR STRING; 212767.Mycsm_02421; -.
DR KEGG; msa:Mycsm_02421; -.
DR PATRIC; fig|710686.3.peg.2438; -.
DR HOGENOM; CLU_033708_0_0_11; -.
DR OrthoDB; 9811352at2; -.
DR Proteomes; UP000010844; Chromosome.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..409
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 560 AA; 59582 MW; 553BA4524AE7EB40 CRC64;
MFTLALIGFL GGVITGISPC ILPVLPVIFF SGAQAGQPKA RPYRVIGGLV LSFSIVTLVG
SALLSLLHLP QDAIRWVALV ALAAIGVGLI FPRVEALLEK PFSRLPQKQF GSGSGGFGLG
LALGVLYVPC AGPVLAAIVI AGATGTVGLP TVALTLSFAV GAALPLLFFA LAGRRVSERV
AAFRRRQGEI RIAAGIVTIL LAVALVFNLP AALQRAIPDY TAKLQETVGG DAQLREKLNL
GGLVNDQNKE LSNCTNGAPE LESCGTAPDL TGITGWLNTP NGAAVDLKSR RGKVVIVDFW
AYSCINCQRA IPHIVDWYHA YKDAGLEVIG VHTPEYAFER VPANVAGGAR DLGITYPVAL
DPNYSTWSNY RNRYWPAKYL IDANGTVRHI KFGEGDYAQT ETIIRQLLSD AHPGIKLPAP
TDAADTTPPP DLTPETYLGV GKVVNYGGTG SYDEGATTYE YPTRLPDDTF AYKGDWKLDY
QGATANAAHS SIELNYRARN VYLVIGGTGT VTVTRDGESM QIPVSGPPAL RQIAADDEVN
RNTLEVQLSQ GLQAFSFTFG
//