(data stored in ACNUC7421 zone)

SWISSPROT: SKFB_BACSU

ID   SKFB_BACSU              Reviewed;         410 AA.
AC   O31423; O31424; O87096; O87097;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   11-DEC-2019, entry version 114.
DE   RecName: Full=Sporulation killing factor maturation protein SkfB;
DE            EC=1.21.98.- {ECO:0000305|PubMed:23282011};
GN   Name=skfB {ECO:0000303|PubMed:12817086}; Synonyms=ybcP, ybcQ;
GN   OrderedLocusNames=BSU01920;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [4]
RP   FUNCTION IN SYNTHESIS OF SKFA, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=12817086; DOI=10.1126/science.1086462;
RA   Gonzalez-Pastor J.E., Hobbs E.C., Losick R.;
RT   "Cannibalism by sporulating bacteria.";
RL   Science 301:510-513(2003).
RN   [5]
RP   REPRESSION BY ABRB AND ABH.
RX   PubMed=17720793; DOI=10.1128/jb.01081-07;
RA   Strauch M.A., Bobay B.G., Cavanagh J., Yao F., Wilson A., Le Breton Y.;
RT   "Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.";
RL   J. Bacteriol. 189:7720-7732(2007).
RN   [6]
RP   FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, AND MUTAGENESIS OF
RP   117-CYS--CYS-124 AND 380-CYS--CYS-387.
RC   STRAIN=168;
RX   PubMed=23282011; DOI=10.1021/ja310542g;
RA   Fluehe L., Burghaus O., Wieckowski B.M., Giessen T.W., Linne U.,
RA   Marahiel M.A.;
RT   "Two [4Fe-4S] clusters containing radical SAM enzyme SkfB catalyze
RT   thioether bond formation during the maturation of the sporulation killing
RT   factor.";
RL   J. Am. Chem. Soc. 135:959-962(2013).
CC   -!- FUNCTION: Catalyzes the formation of the thioether bond required for
CC       production of the sporulation killing factor (SKF) from SkfA
CC       (PubMed:12817086). Forms the cysteine-methionine thioether bond found
CC       in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small
CC       hydrophilic amino acid but not a larger hydrophilic amino acid, i.e.
CC       Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys (PubMed:23282011). The
CC       relative position of Cys and Met in the substrate cannot be inverted,
CC       in vitro the thioether bond cannot be made in the absence of the SkfA
CC       propeptide, suggesting this is the first reaction in SKF maturation
CC       (PubMed:23282011). In vitro, in the absence of a second substrate,
CC       cleaves S-adenosyl-L-methionine into Met and 5'-dA (PubMed:23282011).
CC       {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:23282011}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:23282011};
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine
CC       (PubMed:23282011). The other is coordinated via 3 cysteines and maybe
CC       direct contact with the SkfA precursor (Probable).
CC       {ECO:0000269|PubMed:23282011, ECO:0000305|PubMed:23282011};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23282011}.
CC   -!- INDUCTION: By Spo0A (PubMed:12817086) and PhoP, during nutrient
CC       starvation, especially phosphate starvation. Repressed by AbrB during
CC       normal growth when nutrients are plentiful, in association with the
CC       transcriptional repressor Abh. {ECO:0000269|PubMed:12817086,
CC       ECO:0000269|PubMed:17720793}.
CC   -!- DISRUPTION PHENOTYPE: When the skfA-skfB-skfC-skfE-skfF-skfG-skfH
CC       operon is deleted, increased rate of spore formation; a double operon
CC       deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster
CC       (PubMed:12817086). {ECO:0000269|PubMed:12817086}.
CC   -!- MISCELLANEOUS: Accelerated cannibalism by skf- cells is seen on solid
CC       media but not in liquid media. {ECO:0000269|PubMed:12817086}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA33089.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AB006424; BAA33087.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AB006424; BAA33088.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AB006424; BAA33089.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB11985.2; -; Genomic_DNA.
DR   PIR; D69746; D69746.
DR   PIR; E69746; E69746.
DR   RefSeq; NP_388073.2; NC_000964.3.
DR   RefSeq; WP_003234902.1; NZ_JNCM01000030.1.
DR   PDB; 6EFN; X-ray; 1.29 A; A=1-410.
DR   PDBsum; 6EFN; -.
DR   SMR; O31423; -.
DR   STRING; 224308.BSU01920; -.
DR   PaxDb; O31423; -.
DR   PRIDE; O31423; -.
DR   DNASU; 938501; -.
DR   EnsemblBacteria; CAB11985; CAB11985; BSU01920.
DR   GeneID; 938501; -.
DR   KEGG; bsu:BSU01920; -.
DR   PATRIC; fig|224308.179.peg.199; -.
DR   eggNOG; ENOG4107ZBH; Bacteria.
DR   eggNOG; COG0535; LUCA.
DR   InParanoid; O31423; -.
DR   OMA; EGEMLGC; -.
DR   PhylomeDB; O31423; -.
DR   BioCyc; BSUB:BSU01920-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030152; P:bacteriocin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR030915; rSAM_SkfB.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   SFLD; SFLDF00515; sporulation_killing_factor_pro; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR04403; rSAM_skfB; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31423.
DR   SWISS-2DPAGE; O31423.
KW   3D-structure; 4Fe-4S; Antibiotic biosynthesis; Bacteriocin biosynthesis;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..410
FT                   /note="Sporulation killing factor maturation protein SkfB"
FT                   /id="PRO_0000153049"
FT   METAL           117
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000305|PubMed:23282011"
FT   METAL           121
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000305|PubMed:23282011"
FT   METAL           124
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000305|PubMed:23282011"
FT   METAL           380
FT                   /note="Iron-sulfur (4Fe-4S-S-substrate)"
FT                   /evidence="ECO:0000305|PubMed:23282011"
FT   METAL           385
FT                   /note="Iron-sulfur (4Fe-4S-S-substrate)"
FT                   /evidence="ECO:0000305|PubMed:23282011"
FT   METAL           387
FT                   /note="Iron-sulfur (4Fe-4S-S-substrate)"
FT                   /evidence="ECO:0000305|PubMed:23282011"
FT   MUTAGEN         117..124
FT                   /note="CNLSCSFC->ANLSASFA: No longer cleaves SAM, contains
FT                   55% iron of wild-type."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   MUTAGEN         380..387
FT                   /note="CEAKNCKC->AEAKNAKA: Cleaves SAM, but does not form
FT                   thioether bond, contains 52% iron of wild-type."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   STRAND          14..19
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          22..27
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   TURN            28..30
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          33..36
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           38..50
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           53..64
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           70..77
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           81..85
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   TURN            86..91
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          96..99
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          101..103
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          107..112
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           138..150
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          155..162
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           163..165
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           169..179
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          180..187
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           194..203
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          205..211
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           216..223
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           228..241
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          246..252
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   TURN            254..256
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           257..259
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           260..270
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          273..279
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           284..287
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           295..312
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   TURN            313..315
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          316..318
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   TURN            336..338
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          339..342
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          346..351
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   STRAND          358..360
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   TURN            361..363
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           366..369
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           372..381
FT                   /evidence="ECO:0000244|PDB:6EFN"
FT   HELIX           388..390
FT                   /evidence="ECO:0000244|PDB:6EFN"
SQ   SEQUENCE   410 AA;  45755 MW;  3D243C673E811C0F CRC64;
     MSYDRVKDFD LPELAVHLQP HGAVMIDRKS MFYFRLSGRG AQLAFLLSKN KNLHKTARIW
     EIMKKEEMSA DQLKEELSAH PFTEAWTEGL LDQPLHVSGS LDSYLPISCT LQLTNACNLS
     CSFCYASSGK PYPEELSSEQ WILVMQKLAA HGVADITLTG GEAKLIKGFK ELVVVASSLF
     TNVNVFSNGL NWRDEEVELL SHLGNVSVQI SIDGMDNTHD QLRGRKGGFK ESMNTIKKLS
     EANIPVIVAM TINESNADEV SDVVEQCANA GAFIFRAGKT LSVGRATEGF KALDIDFEEM
     VQIQLREARH KWGDRLNIID WEHEESSFTT DFCTPGYLAW YIRADGYVTP CQLEDLPLGH
     ILEDSMADIG SPARLLQLKC EAKNCKCIGK IELSEPDLPF QKEVKAGIQE
//

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