YODP_BACSU
ID YODP_BACSU Reviewed; 275 AA.
AC O34895; Q796B4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=N-acetyltransferase YodP {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:21538109};
DE AltName: Full=Beta-lysine N(6)-acetyltransferase {ECO:0000305};
DE EC=2.3.1.264 {ECO:0000269|PubMed:21538109};
GN Name=yodP; Synonyms=yokR; OrderedLocusNames=BSU19700;
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;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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 INDUCTION.
RX PubMed=10869437; DOI=10.1073/pnas.140209597;
RA Fawcett P., Eichenberger P., Losick R., Youngman P.;
RT "The transcriptional profile of early to middle sporulation in Bacillus
RT subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8063-8068(2000).
RN [4]
RP INDUCTION.
RX PubMed=14523133; DOI=10.1099/mic.0.26413-0;
RA Feucht A., Evans L., Errington J.;
RT "Identification of sporulation genes by genome-wide analysis of the sigmaE
RT regulon of Bacillus subtilis.";
RL Microbiology 149:3023-3034(2003).
RN [5]
RP FUNCTION AS AN ACETYLTRANSFERASE, CATALYTIC ACTIVITY, BIOTECHNOLOGY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=21538109; DOI=10.1007/s00253-011-3301-8;
RA Muller S., Hoffmann T., Santos H., Saum S.H., Bremer E., Muller V.;
RT "Bacterial abl-like genes: production of the archaeal osmolyte N(epsilon)-
RT acetyl-beta-lysine by homologous overexpression of the yodP-kamA genes in
RT Bacillus subtilis.";
RL Appl. Microbiol. Biotechnol. 91:689-697(2011).
CC -!- FUNCTION: In vitro, is able to catalyze the acetylation of beta-lysine
CC to N6-acetyl-beta-lysine, an archaeal osmolyte produced by methanogenic
CC archaea. Its physiological function has not yet been elucidated.
CC {ECO:0000269|PubMed:21538109}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3,6-diaminohexanoate + acetyl-CoA = (3S)-6-acetamido-3-
CC aminohexanoate + CoA + H(+); Xref=Rhea:RHEA:33019, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57434,
CC ChEBI:CHEBI:137165; EC=2.3.1.264;
CC Evidence={ECO:0000269|PubMed:21538109};
CC -!- INDUCTION: Up-regulated during sporulation, under the control of the
CC sigma-E transcription factor (SigE). {ECO:0000269|PubMed:10869437,
CC ECO:0000269|PubMed:14523133}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the genomic region encompassing the
CC entire yodT-yodS-yodR-yodQ-yodP-kamA gene cluster has no noticeable
CC effect on growth either in rich or minimal medium, does not affect
CC sporulation, and does not cause osmotic sensitivity or influence the
CC compatible solute pool of this soil bacterium.
CC {ECO:0000269|PubMed:21538109}.
CC -!- BIOTECHNOLOGY: The use of YodP from B.subtilis for N6-acetyl-beta-
CC lysine synthesis opens the bottleneck for the large-scale production of
CC N6-acetyl-beta-lysine to investigate its properties as a compatible
CC solute. {ECO:0000269|PubMed:21538109}.
CC -!- MISCELLANEOUS: N6-acetyl-beta-lysine is not synthesized by B.subtilis
CC as part of its cellular defense against high salinity.
CC {ECO:0000305|PubMed:21538109}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AF006665; AAB81158.1; -; Genomic_DNA.
DR EMBL; AF015775; AAB72070.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13861.1; -; Genomic_DNA.
DR PIR; C69904; C69904.
DR RefSeq; NP_389851.1; NC_000964.3.
DR RefSeq; WP_004399564.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34895; -.
DR STRING; 224308.BSU19700; -.
DR PaxDb; O34895; -.
DR PRIDE; O34895; -.
DR EnsemblBacteria; CAB13861; CAB13861; BSU_19700.
DR GeneID; 940057; -.
DR KEGG; bsu:BSU19700; -.
DR PATRIC; fig|224308.179.peg.2157; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; O34895; -.
DR OMA; LESMNVW; -.
DR BioCyc; BSUB:BSU19700-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR022525; GNAT_AblB.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR03827; GNAT_ablB; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..275
FT /note="N-acetyltransferase YodP"
FT /id="PRO_0000360500"
FT DOMAIN 125..271
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 275 AA; 31221 MW; 3F663053A09B6730 CRC64;
MLKSIKSSGV TAVLDHDGFN KRIRVVRYDG AIEKALPDIV AAAKEENAEK IIVYAKQHDE
PILAKQLFAP EGYLKGYYLG HSACVMVRYL SESRRQTDSY TEEQEIIEAI YRTAPRLRND
STPVFTMRKA ETNDMYQLSM LYKKVFRTYP TPVFDPAYIE KTMNANTVYY IMLDHDRLIS
AASAEINPEL GHAEITDCAV LPEYRGHSLT SFLIEALEKE MAGEDIVHVF SLARASSFGM
NAVLYHSGYQ YGGRLINNCF IAEGLENMNI WCKQL
