ID   SBNA_STAAB              Reviewed;         326 AA.
AC   Q2YUU0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   01-MAY-2013, entry version 56.
DE   RecName: Full=Probable siderophore biosynthesis protein SbnA;
GN   Name=sbnA; OrderedLocusNames=SAB0055;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Probable pyridoxal phosphate-dependent enzyme involved
CC       in siderophore biosynthesis (By similarity).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- INDUCTION: Up-regulated under iron-deficient growth conditions.
CC       Repressed by Fur under iron-rich growth conditions (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family.
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DR   EMBL; AJ938182; CAI79743.1; -; Genomic_DNA.
DR   RefSeq; YP_415571.1; NC_007622.1.
DR   STRING; 273036.SAB0055; -.
DR   EnsemblBacteria; CAI79743; CAI79743; SAB0055.
DR   GeneID; 3794556; -.
DR   KEGG; sab:SAB0055; -.
DR   PATRIC; 19520799; VBIStaAur92441_0068.
DR   eggNOG; COG0031; -.
DR   HOGENOM; HOG000217394; -.
DR   KO; K01738; -.
DR   OMA; NAVWINQ; -.
DR   ProtClustDB; CLSK884408; -.
DR   BioCyc; SAUR273036:GJVS-57-MONOMER; -.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   InterPro; IPR001216; Cys_synth_BS.
DR   InterPro; IPR023927; DiNH2opropionate_SbnA.
DR   InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1.
DR   TIGRFAMs; TIGR03945; PLP_SbnA_fam; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Pyridoxal phosphate.
FT   CHAIN         1    326       Probable siderophore biosynthesis protein
FT                                SbnA.
FT                                /FTId=PRO_0000395011.
FT   REGION      185    189       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      77     77       Pyridoxal phosphate (By similarity).
FT   BINDING     272    272       Pyridoxal phosphate (By similarity).
FT   MOD_RES      47     47       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   326 AA;  35995 MW;  21671D5F66E7F8E9 CRC64;
     MIEKSQACHD SLLDSVGQTP MVQLHQLFPK HEVFAKLEYM NPGGSMKDRP AKYIIEHGIK
     HGLITENTHL IESTSGNLGI ALAMIAKIKG LKLTCVVDPK ISPTNLKIIK SYGVNVEMVE
     EPDAHGGYLM TRIAKVQELL ATIEDAYWIN QYANELNWQS HYHGAGTEIV ETIKQPIDYF
     VAPVSTTGSI MGMSRKIKEV HPNVQIVAVD AKGSVIFGDK PINRELPGIG ASRVPEILNR
     SEINQVIHVD DYQSALGCRK LIDYEGIFAG GSTGSIIVAI EQLITSIEEG ATIVTILPDR
     GDRYLDLVYS DTWLEKMKSR QGVKSE
//