ID   BLAP_BACSU              Reviewed;          73 AA.
AC   C0H419; Q9R9I3;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Biotin/lipoyl attachment protein;
DE            Short=BLAP;
GN   Name=yngHB; OrderedLocusNames=BSU18239;
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=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=10557314; DOI=10.1073/pnas.96.23.13294;
RA   Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W.,
RA   Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F.,
RA   Vater J.;
RT   "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT   multifunctional hybrid between a peptide synthetase, an amino transferase,
RT   and a fatty acid synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999).
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   STRUCTURE BY NMR OF 2-73 OF THE APO- AND BIOTINYLATED FORMS, BIOTINYLATION
RP   AT LYS-35, LIPOYLATION AT LYS-35, INDUCTION, MASS SPECTROMETRY, AND
RP   MUTAGENESIS OF TRP-12.
RC   STRAIN=168;
RX   PubMed=16699181; DOI=10.1074/jbc.m602660200;
RA   Cui G., Nan B., Hu J., Wang Y., Jin C., Xia B.;
RT   "Identification and solution structures of a single domain biotin/lipoyl
RT   attachment protein from Bacillus subtilis.";
RL   J. Biol. Chem. 281:20598-20607(2006).
CC   -!- INDUCTION: Detected in log-phase B.subtilis cells (at protein level).
CC       {ECO:0000269|PubMed:16699181}.
CC   -!- PTM: Can be both biotinylated and lipoylated on Lys-35 upon
CC       overexpression in E.coli depending on the growth medium; the nature of
CC       the modification in situ in B.subtilis is unknown.
CC       {ECO:0000269|PubMed:16699181}.
CC   -!- MASS SPECTROMETRY: Mass=7913; Method=Unknown; Note=Upon overexpression
CC       in E.coli.; Evidence={ECO:0000269|PubMed:16699181};
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DR   EMBL; AF184956; AAF08803.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAX52627.1; -; Genomic_DNA.
DR   PIR; T44814; T44814.
DR   RefSeq; WP_003245519.1; NZ_JNCM01000035.1.
DR   RefSeq; YP_003097733.1; NC_000964.3.
DR   PDB; 1Z6H; NMR; -; A=2-73.
DR   PDB; 1Z7T; NMR; -; A=2-73.
DR   PDB; 2B8F; NMR; -; A=2-73.
DR   PDB; 2B8G; NMR; -; A=2-73.
DR   PDBsum; 1Z6H; -.
DR   PDBsum; 1Z7T; -.
DR   PDBsum; 2B8F; -.
DR   PDBsum; 2B8G; -.
DR   AlphaFoldDB; C0H419; -.
DR   BMRB; C0H419; -.
DR   SMR; C0H419; -.
DR   STRING; 224308.BSU18239; -.
DR   DrugBank; DB07497; 5-(hexahydro-2-oxo-1H-thieno[3,4-D]imidazol-6-yl)pentanal.
DR   PaxDb; C0H419; -.
DR   EnsemblBacteria; CAX52627; CAX52627; BSU_18239.
DR   GeneID; 8303012; -.
DR   KEGG; bsu:BSU18239; -.
DR   PATRIC; fig|224308.179.peg.1989; -.
DR   eggNOG; COG0511; Bacteria.
DR   InParanoid; C0H419; -.
DR   OMA; MAGNLWK; -.
DR   PhylomeDB; C0H419; -.
DR   BioCyc; BSUB:BSU18239-MON; -.
DR   EvolutionaryTrace; C0H419; -.
DR   Proteomes; UP000001570; Chromosome.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Biotin; Lipoyl; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..73
FT                   /note="Biotin/lipoyl attachment protein"
FT                   /id="PRO_0000389494"
FT   DOMAIN          2..69
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         35
FT                   /note="N6-biotinyllysine; alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:16699181"
FT   MOD_RES         35
FT                   /note="N6-lipoyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:16699181"
FT   VARIANT         4
FT                   /note="S -> I (in strain: ATCC 6633)"
FT   VARIANT         21
FT                   /note="Q -> H (in strain: ATCC 6633)"
FT   VARIANT         47
FT                   /note="I -> T (in strain: ATCC 6633)"
FT   VARIANT         54
FT                   /note="K -> N (in strain: ATCC 6633)"
FT   VARIANT         70
FT                   /note="N -> D (in strain: ATCC 6633)"
FT   MUTAGEN         12
FT                   /note="W->M: No changes in biotinylation in E.coli."
FT                   /evidence="ECO:0000269|PubMed:16699181"
FT   STRAND          7..14
FT                   /evidence="ECO:0007829|PDB:1Z6H"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:1Z6H"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:1Z6H"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:1Z6H"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:1Z6H"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:1Z6H"
SQ   SEQUENCE   73 AA;  8041 MW;  0358FB92D5DBED91 CRC64;
     MTVSIQMAGN LWKVHVKAGD QIEKGQEVAI LESMKMEIPI VADRSGIVKE VKKKEGDFVN
     EGDVLLELSN STQ