ID   TRPB_STAES              Reviewed;         402 AA.
AC   Q8CPB1;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=SE_1053;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
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DR   EMBL; AE015929; AAO04650.1; -; Genomic_DNA.
DR   RefSeq; NP_764608.1; NC_004461.1.
DR   RefSeq; WP_001831324.1; NZ_WBME01000002.1.
DR   AlphaFoldDB; Q8CPB1; -.
DR   SMR; Q8CPB1; -.
DR   STRING; 176280.SE_1053; -.
DR   EnsemblBacteria; AAO04650; AAO04650; SE_1053.
DR   GeneID; 50018820; -.
DR   KEGG; sep:SE_1053; -.
DR   PATRIC; fig|176280.10.peg.1029; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_9; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00263; trpB; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           1..402
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099003"
FT   MOD_RES         92
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   402 AA;  43834 MW;  0696BF8E8FB25CFB CRC64;
     MKIQTEVDEL GFFGEYGGQY VPETLMPAII ELKKAYEDAK SDTHFKKEFN YYLSEYVGRE
     TPLTFAESYT KLLGGAKIYL KREDLNHTGA HKINNAIGQA LLAKRMGKTK LVAETGAGQH
     GVASATIAAL FDMDLIVFMG SEDIKRQQLN VFRMELLGAK VVSVSDGQGT LSDAVNKALQ
     YWVNHVEDTH YLLGSALGPD PFPTMVRDFQ SVIGNEIKSQ ILSKEGRLPD ALVACVGGGS
     NSIGTFYPFI QDDVKLYGVE AAGKGSHTHN HALAIGKGKP GVLHGSKMYL IQNDDGQIEL
     AHSISAGLDY PGIGPEHSYY NDIGRVSYVS ATDNEAMEAL ITFSKVEGII PAIESAHALS
     YVEKLAPNMD EKEIIVVTIS GRGDKDMETI KQYKENGGEQ NE