ID   Y6410_MYCS2             Reviewed;         518 AA.
AC   A0R635; I7FUS9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative Rieske 2Fe-2S iron-sulfur protein MSMEG_6410/MSMEI_6242;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=MSMEG_6410, MSMEI_6242;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-375, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
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DR   EMBL; CP000480; ABK76191.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42668.1; -; Genomic_DNA.
DR   RefSeq; WP_011731268.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890623.1; NC_008596.1.
DR   AlphaFoldDB; A0R635; -.
DR   SMR; A0R635; -.
DR   STRING; 246196.MSMEI_6242; -.
DR   EnsemblBacteria; ABK76191; ABK76191; MSMEG_6410.
DR   EnsemblBacteria; AFP42668; AFP42668; MSMEI_6242.
DR   GeneID; 66737687; -.
DR   KEGG; msg:MSMEI_6242; -.
DR   KEGG; msm:MSMEG_6410; -.
DR   PATRIC; fig|246196.19.peg.6236; -.
DR   eggNOG; COG2146; Bacteria.
DR   eggNOG; COG2220; Bacteria.
DR   OMA; DGWEIQR; -.
DR   OrthoDB; 767622at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 2.102.10.10; -; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Iron; Iron-sulfur; Isopeptide bond; Metal-binding; Oxidoreductase;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..518
FT                   /note="Putative Rieske 2Fe-2S iron-sulfur protein
FT                   MSMEG_6410/MSMEI_6242"
FT                   /id="PRO_0000396105"
FT   DOMAIN          431..518
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         471
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         473
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         491
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         494
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   CROSSLNK        375
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   518 AA;  58638 MW;  0F01FD0A2F30C4EF CRC64;
     MQVTSVGHAG FLIESRAGSI LCDPWVNPAY FASWFPFPDN SQLDWDALGD VDYLYVSHLH
     KDHFDPEHLR RYVNKDAVVL LPDYPVPDLR RELEKLGFHN FFETTDSVKH TVSGPKGDLD
     VMIIALRAPA DGPIGDSGLV VSDRVTTVFN MNDARPVDLD VLHTDFGQID VHMLQYSGAI
     WYPMVYDMPA RAKEAFGIQK RQRQMDRCRQ YIAQVGATWV VPSAGPPCFL DPELRDLNDD
     HGDPANIFPD QMVFLEQLRI HGHDGGLLMI PGSTADFTGS TLNSLTHPVD DPESIFTTGK
     AAYIEDYAQR MAPVLAAEKA RWAPSAGEPM LEALRALFEP IMTQTDQICD GIGYPVELRL
     TGRDHNETVV LDFPKRVVRE PIPDEKFRYG FEIPAALVRT VLRDEEPDWV NTIFLSTRFR
     AWRVGGYNEY LYTFFKCLTD ERIAYADGWF AEAHDDSSSI TLDGFQIQRR CPHLKADLSK
     FGVVEGNTLT CNLHGWQWNL ENGRCLTTKG HELRCQKL