ID   EPSN_BACSU              Reviewed;         388 AA.
AC   Q795J3; O08182; P71064;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Putative pyridoxal phosphate-dependent aminotransferase EpsN;
DE            EC=2.6.1.-;
GN   Name=epsN; Synonyms=yvfE; OrderedLocusNames=BSU34230;
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   PROBABLE FUNCTION, AND 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).
CC   -!- FUNCTION: May be involved in the production of the exopolysaccharide
CC       (EPS) component of the extracellular matrix during biofilm formation.
CC       EPS is responsible for the adhesion of chains of cells into bundles.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- INDUCTION: Repressed by SinR. {ECO:0000269|PubMed:15661000}.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA96482.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB07998.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z71928; CAA96482.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z94043; CAB07998.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB15428.2; -; Genomic_DNA.
DR   PIR; F70037; F70037.
DR   RefSeq; NP_391303.2; NC_000964.3.
DR   RefSeq; WP_009968194.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; Q795J3; -.
DR   SMR; Q795J3; -.
DR   STRING; 224308.BSU34230; -.
DR   PaxDb; Q795J3; -.
DR   EnsemblBacteria; CAB15428; CAB15428; BSU_34230.
DR   GeneID; 936364; -.
DR   KEGG; bsu:BSU34230; -.
DR   PATRIC; fig|224308.179.peg.3710; -.
DR   eggNOG; COG0399; Bacteria.
DR   InParanoid; Q795J3; -.
DR   OMA; RFWATQA; -.
DR   PhylomeDB; Q795J3; -.
DR   BioCyc; BSUB:BSU34230-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244; PTHR30244; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Exopolysaccharide synthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..388
FT                   /note="Putative pyridoxal phosphate-dependent
FT                   aminotransferase EpsN"
FT                   /id="PRO_0000360687"
FT   MOD_RES         190
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  42924 MW;  56DE09C304DDB491 CRC64;
     MHKKIYLSPP HMSGREQHYI SEAFRSNWIA PLGPLVNSFE EQLAERVGVK AAAAVGSGTA
     AIHLALRLLE VKEGDSVFCQ SFTFVATANP ILYEKAVPVF IDSEPDTWNM SPTALERALE
     EAKRNGTLPK AVIAVNLYGQ SAKMDEIVSL CDAYGVPVIE DAAESLGTVY KGKQSGTFGR
     FGIFSFNGNK IITTSGGGML VSNDEAAIEK ARFLASQARE PAVHYQHSEI GHNYRLSNIL
     AGVGIAQLEV LDERVEKRRT IFTRYKNALG HLDGVRFMPE YAAGVSNRWL TTLTLDNGLS
     PYDIVQRLAE ENIEARPLWK PLHTQPLFDP ALFYSHEDTG SVCEDLFKRG ICLPSGSNMT
     EDEQGRVIEV LLHLFHTVEV KKWTASIR