ID   Y285_HELPJ              Reviewed;         418 AA.
AC   Q9ZMF0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative methylthiotransferase jhp_0270;
DE            EC=2.-.-.-;
GN   OrderedLocusNames=jhp_0270;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00780};
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|PROSITE-ProRule:PRU00780};
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05851.1; -; Genomic_DNA.
DR   PIR; G71952; G71952.
DR   RefSeq; WP_000758501.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZMF0; -.
DR   SMR; Q9ZMF0; -.
DR   STRING; 85963.jhp_0270; -.
DR   EnsemblBacteria; AAD05851; AAD05851; jhp_0270.
DR   KEGG; hpj:jhp_0270; -.
DR   eggNOG; COG0621; Bacteria.
DR   OMA; HFHIPLQ; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.12160; -; 1.
DR   Gene3D; 3.80.30.20; -; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR038135; Methylthiotransferase_N_sf.
DR   InterPro; IPR006467; MiaB-like_C.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR01579; MiaB-like-C; 1.
DR   TIGRFAMs; TIGR00089; TIGR00089; 1.
DR   PROSITE; PS51449; MTTASE_N; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..418
FT                   /note="Putative methylthiotransferase jhp_0270"
FT                   /id="PRO_0000141743"
FT   DOMAIN          2..110
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   DOMAIN          130..355
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   BINDING         45
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   BINDING         144
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   BINDING         148
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT   BINDING         151
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ   SEQUENCE   418 AA;  47962 MW;  5661FE45D29AF33E CRC64;
     MKKVYFKTFG CRTNLFDTQV MGENLKDFSA TLEEQEADII IINSCTVTNG TDSAVRSYAR
     KMARLDKEVL FTGCGVKTQG KELFEKGLLK GVFGHDNKEK INALLQEKKR FFIDDNLENK
     HLDTTMVSEF VGKTRAFIKI QEGCDFDCNY CIIPSVRGRA RSFEERKILE QVGLLCSKGV
     QEVVLTGTNV GSYGKDRGSN IARLIKKLSQ ITGLKRIRIG SLEPNQINDE FLELLEEDFL
     EKHLHIALQH SHDFMLERMN RRNRTKSDRE LLEIIASKNF AIGTDFIVGH PGESESVFEK
     AFKNLESLPL THIHPFIYSK RKDTPSSLMR DSVSLEDSKK RLNAIKDLIF HKNKAFRQLQ
     LKLNTPLKAL VEAQKDGEFK ALDQFFNPIK IKSDKPLRAS FLEIKEYEIK ERENHAVF