EPSM_BACSU
ID EPSM_BACSU Reviewed; 216 AA.
AC P71063; O08181; Q795J2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=UDP-N-acetylbacillosamine N-acetyltransferase {ECO:0000305};
DE EC=2.3.1.203 {ECO:0000269|PubMed:30314705};
GN Name=epsM {ECO:0000303|PubMed:15661000}; Synonyms=yvfD;
GN OrderedLocusNames=BSU34240;
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=8969506; DOI=10.1099/13500872-142-11-3089;
RA Fabret C., Quentin Y., Chapal N., Guiseppi A., Haiech J., Denizot F.;
RT "Integrated mapping and sequencing of a 115 kb DNA fragment from Bacillus
RT subtilis: sequence analysis of a 21 kb segment containing the sigL locus.";
RL Microbiology 142:3089-3096(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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).
RN [4]
RP INDUCTION.
RX PubMed=15661000; DOI=10.1111/j.1365-2958.2004.04440.x;
RA Kearns D.B., Chu F., Branda S.S., Kolter R., Losick R.;
RT "A master regulator for biofilm formation by Bacillus subtilis.";
RL Mol. Microbiol. 55:739-749(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=20720312; DOI=10.1007/bf03208867;
RA Nagorska K., Ostrowski A., Hinc K., Holland I.B., Obuchowski M.;
RT "Importance of eps genes from Bacillus subtilis in biofilm formation and
RT swarming.";
RL J. Appl. Genet. 51:369-381(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF HIS-146.
RC STRAIN=168;
RX PubMed=30314705; DOI=10.1016/j.bbrc.2018.09.185;
RA Kaundinya C.R., Savithri H.S., Rao K.K., Balaji P.V.;
RT "EpsM from Bacillus subtilis 168 has UDP-2,4,6-trideoxy-2-acetamido-4-amino
RT glucose acetyltransferase activity in vitro.";
RL Biochem. Biophys. Res. Commun. 505:1057-1062(2018).
CC -!- FUNCTION: Catalyzes the conversion of UDP-2,4,6-trideoxy-2-acetamido-4-
CC amino glucose to UDP-2,4,6-trideoxy-2,4-diacetamido glucose, commonly
CC known as UDP-N,N'-diacetylbacillosamine (UDP-diNAcBac).
CC {ECO:0000269|PubMed:30314705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + UDP-N-acetylbacillosamine = CoA + H(+) + UDP-
CC N,N'-diacetylbacillosamine; Xref=Rhea:RHEA:34159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:63277,
CC ChEBI:CHEBI:67134; EC=2.3.1.203;
CC Evidence={ECO:0000269|PubMed:30314705};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70.73 uM for UDP-N-acetylbacillosamine
CC {ECO:0000269|PubMed:30314705};
CC -!- SUBUNIT: Forms oligomers. {ECO:0000269|PubMed:30314705}.
CC -!- INDUCTION: Repressed by SinR. {ECO:0000269|PubMed:15661000}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant shows decreased efficiency of
CC biofilm formation. Disruption affects swarming motility.
CC {ECO:0000269|PubMed:20720312}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; Z71928; CAA96481.1; -; Genomic_DNA.
DR EMBL; Z94043; CAB07997.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15429.1; -; Genomic_DNA.
DR PIR; E70037; E70037.
DR RefSeq; NP_391304.1; NC_000964.3.
DR RefSeq; WP_003228268.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P71063; -.
DR SMR; P71063; -.
DR STRING; 224308.BSU34240; -.
DR PaxDb; P71063; -.
DR EnsemblBacteria; CAB15429; CAB15429; BSU_34240.
DR GeneID; 936372; -.
DR KEGG; bsu:BSU34240; -.
DR PATRIC; fig|224308.179.peg.3711; -.
DR eggNOG; COG0110; Bacteria.
DR InParanoid; P71063; -.
DR OMA; GAHCIIN; -.
DR PhylomeDB; P71063; -.
DR BioCyc; BSUB:BSU34240-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd03360; LbH_AT_putative; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR041561; PglD_N.
DR InterPro; IPR020019; Sia_OAcTrfase_NeuD-like.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF17836; PglD_N; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR03570; NeuD_NnaD; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..216
FT /note="UDP-N-acetylbacillosamine N-acetyltransferase"
FT /id="PRO_0000360686"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q0P9D1"
FT BINDING 146
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q0P9D1"
FT MUTAGEN 146
FT /note="H->L: Loss of activity. Affects the oligomeric
FT state."
FT /evidence="ECO:0000269|PubMed:30314705"
SQ SEQUENCE 216 AA; 22483 MW; 37E6B4076A480F76 CRC64;
MKNVAIVGDG GHGKVIRELI NARSDTRLAA VLDDKFKTFE GGKEWYTGPP KAVTELRRLI
PDVLFLIAVG NNSVRKQLAE RLGLGKDDFI TLIHPSAIVS KSAVIGEGTV IMAGAIIQAD
ARIGAHCIIN TGAVAEHDNQ ISDYVHLSPR ATLSGAVSVQ EGAHVGTGAS VIPQIIIGAW
SIVGAGSAVI RSIPDRVTAA GAPARIISSI QTSNKG
