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Database: UniProt/TrEMBL
Entry: B2TW97_SHIB3
LinkDB: B2TW97_SHIB3
Original site: B2TW97_SHIB3 
ID   B2TW97_SHIB3            Unreviewed;       422 AA.
AC   B2TW97;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   01-OCT-2014, entry version 45.
DE   RecName: Full=Bifunctional protein FolC {ECO:0000256|PIRNR:PIRNR001563};
GN   Name=folC {ECO:0000313|EMBL:ACD06395.1};
GN   OrderedLocusNames=SbBS512_E2693 {ECO:0000313|EMBL:ACD06395.1};
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609 {ECO:0000313|EMBL:ACD06395.1, ECO:0000313|Proteomes:UP000001030};
RN   [1] {ECO:0000313|Proteomes:UP000001030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512 {ECO:0000313|Proteomes:UP000001030};
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conversion of folates to polyglutamate derivatives.
CC       {ECO:0000256|PIRNR:PIRNR001563}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001563}.
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DR   EMBL; CP001063; ACD06395.1; -; Genomic_DNA.
DR   RefSeq; YP_001881137.1; NC_010658.1.
DR   ProteinModelPortal; B2TW97; -.
DR   SMR; B2TW97; 6-419.
DR   STRING; 344609.SbBS512_E2693; -.
DR   EnsemblBacteria; ACD06395; ACD06395; SbBS512_E2693.
DR   GeneID; 6272678; -.
DR   KEGG; sbc:SbBS512_E2693; -.
DR   PATRIC; 18672446; VBIShiBoy129590_2982.
DR   eggNOG; COG0285; -.
DR   HOGENOM; HOG000019982; -.
DR   KO; K11754; -.
DR   OMA; HRDVASA; -.
DR   OrthoDB; EOG6ZPSW2; -.
DR   BioCyc; SBOY344609:GI0O-2691-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   PANTHER; PTHR11136; PTHR11136; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01499; folC; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001563,
KW   ECO:0000256|SAAS:SAAS00031722};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001030};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001563, ECO:0000313|EMBL:ACD06395.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563,
KW   ECO:0000256|SAAS:SAAS00031735}.
SQ   SEQUENCE   422 AA;  45363 MW;  C4BDD5F7ED364FC2 CRC64;
     MIIKRTPQAA SPLASWLSYL ENLHSKTIDL GLERVSQVAA RLGVLKPAPF VFTVAGTNGK
     GTTCRTLESI LMAAGYKVGV YSSPHLVRYT ERVRVQGQEL PESAHTASFA EIESARGDIS
     LTYFEYGTLS ALWLFKQAQL DVVILEVGLG GRLDATNIVD ADVAVVTSIA LDHTDWLGPD
     RESIGREKAG IFRSAKPAIV GEPEMPSTIA DVAQEKGALL QRRGVEWNYS VTDHDWAFSD
     AHGTLENLPL PLVPQPNAAT ALAALRASGL EVSENAIRDG IASAILPGRF QIVSESPRVI
     FDVAHNPHAA EYLTGRMKAL PKNGRVLAVI GMLHDKDIAG TLAWLKSVVD DWYCAPLEGP
     RGATAEQLLE HLGNGKSFDS VAQAWDAAMA DAKAEDTVLV CGSFHTVAHV MEVIDARRSG
     GK
//
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