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Database: UniProt
Entry: Q7A1Z6
LinkDB: Q7A1Z6
Original site: Q7A1Z6 
ID   SBNA_STAAW              Reviewed;         326 AA.
AC   Q7A1Z6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   26-NOV-2014, entry version 69.
DE   RecName: Full=Probable siderophore biosynthesis protein SbnA;
GN   Name=sbnA; OrderedLocusNames=MW0089;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Probable pyridoxal phosphate-dependent enzyme involved
CC       in siderophore biosynthesis. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- INDUCTION: Up-regulated under iron-deficient growth conditions.
CC       Repressed by Fur under iron-rich growth conditions (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB93954.1; -; Genomic_DNA.
DR   RefSeq; NP_644904.1; NC_003923.1.
DR   ProteinModelPortal; Q7A1Z6; -.
DR   SMR; Q7A1Z6; 9-305.
DR   STRING; 196620.MW0089; -.
DR   EnsemblBacteria; BAB93954; BAB93954; BAB93954.
DR   GeneID; 1004835; -.
DR   KEGG; sam:MW0089; -.
DR   PATRIC; 19566624; VBIStaAur44266_0094.
DR   eggNOG; COG0031; -.
DR   HOGENOM; HOG000217394; -.
DR   KO; K01738; -.
DR   OMA; HAEMTAK; -.
DR   OrthoDB; EOG6Q2SP8; -.
DR   BioCyc; SAUR196620:GJ9Z-91-MONOMER; -.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR023927; SbnA.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 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_0000395021.
FT   REGION      185    189       Pyridoxal phosphate binding.
FT                                {ECO:0000250}.
FT   BINDING      77     77       Pyridoxal phosphate. {ECO:0000250}.
FT   BINDING     272    272       Pyridoxal phosphate. {ECO:0000250}.
FT   MOD_RES      47     47       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   326 AA;  35897 MW;  E682FB5D5E5F76AF CRC64;
     MIEKSQACHD SLLDSVGQTP MVQLHQLFPK HEVFAKLEYM NPGGSMKDRP AKYIIEHGIK
     HGLITENTHL IESTSGNLGI ALAMIAKIKG LKLTCVVDPK ISPTNLKIIK SYGANVEMVE
     EPDAHGGYLM TRIAKVQELL ATIDDAYWIN QYANELNWQS HYHGAGTEIV ETIKQPIDYF
     VAPVSTTGSI MGMSRKIKEV HPNAQIVAVD AKGSVIFGDK PINRELPGIG ASRVPEILNR
     SEINQVIHVD DYQSALGCRK LIDYEGIFAG GSTGSIIAAI EQLITSIEEG ATIVTILPDR
     GDRYLDLVYS DTWLEKMKSR QGVKSE
//
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