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 01-MAY-2013, entry version 61.
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 (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; BA000033; BAB93954.1; -; Genomic_DNA.
DR RefSeq; NP_644904.1; NC_003923.1.
DR HSSP; Q9WZD3; 1O58.
DR ProteinModelPortal; Q7A1Z6; -.
DR SMR; Q7A1Z6; 16-308.
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; NAVWINQ; -.
DR ProtClustDB; CLSK884408; -.
DR BioCyc; SAUR196620:GJ9Z-91-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_0000395021.
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; 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
//
