RIBT_BACSU
ID RIBT_BACSU Reviewed; 124 AA.
AC P17622;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein RibT;
DE EC=2.3.1.-;
GN Name=ribT; OrderedLocusNames=BSU23240;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT "The organization of the Bacillus subtilis 168 chromosome region between
RT the spoVA and serA genetic loci, based on sequence data.";
RL Mol. Microbiol. 10:385-395(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / SHGW;
RA Mironov V.N.;
RL Thesis (1989), USSR Academy of Sciences, Russia.
RN [3]
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).
CC -!- FUNCTION: Involved in riboflavin biosynthesis.
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DR EMBL; L09228; AAA67485.1; -; Genomic_DNA.
DR EMBL; X51510; CAA35882.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14256.1; -; Genomic_DNA.
DR PIR; S45547; S45547.
DR RefSeq; NP_390205.1; NC_000964.3.
DR RefSeq; WP_003223910.1; NZ_JNCM01000036.1.
DR PDB; 5XXR; X-ray; 2.65 A; A/B=1-124.
DR PDB; 5XXS; X-ray; 2.09 A; A/B=1-124.
DR PDBsum; 5XXR; -.
DR PDBsum; 5XXS; -.
DR AlphaFoldDB; P17622; -.
DR SMR; P17622; -.
DR STRING; 224308.BSU23240; -.
DR jPOST; P17622; -.
DR PaxDb; P17622; -.
DR PRIDE; P17622; -.
DR EnsemblBacteria; CAB14256; CAB14256; BSU_23240.
DR GeneID; 50137178; -.
DR GeneID; 64304105; -.
DR GeneID; 938948; -.
DR KEGG; bsu:BSU23240; -.
DR PATRIC; fig|224308.179.peg.2531; -.
DR eggNOG; COG0456; Bacteria.
DR OMA; KLINKWR; -.
DR PhylomeDB; P17622; -.
DR BioCyc; BSUB:BSU23240-MON; -.
DR PRO; PR:P17622; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Riboflavin biosynthesis;
KW Transferase.
FT CHAIN 1..124
FT /note="Protein RibT"
FT /id="PRO_0000097330"
FT DOMAIN 3..124
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5XXS"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5XXS"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:5XXS"
FT HELIX 26..38
FT /evidence="ECO:0007829|PDB:5XXS"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:5XXS"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:5XXS"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:5XXS"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5XXS"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5XXR"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:5XXS"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:5XXS"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5XXS"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5XXS"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:5XXS"
SQ SEQUENCE 124 AA; 14574 MW; 355BD032899572AE CRC64;
MLIRYKKSFE KIAMGLLSFM PNEKDLKQLQ QTIKDYETDT DRQLFLWKED EDIVGAIGVE
KKDSEVEIRH ISVNPSHRHQ GIGKQMMDAL KHLFKTQVLV PNELTQSFFE RCQGQQDQDI
SYNN
