ID   SBNF_STAA8              Reviewed;         616 AA.
AC   Q2G1M8; Q6X7U2;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase {ECO:0000305};
DE            EC=6.3.2.55 {ECO:0000269|PubMed:19775248};
DE   AltName: Full=Staphyloferrin B biosynthesis protein SbnF {ECO:0000305};
GN   Name=sbnF {ECO:0000303|PubMed:14688077};
GN   OrderedLocusNames=SAOUHSC_00080 {ECO:0000312|EMBL:ABD29263.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=14688077; DOI=10.1128/iai.72.1.29-37.2004;
RA   Dale S.E., Doherty-Kirby A., Lajoie G., Heinrichs D.E.;
RT   "Role of siderophore biosynthesis in virulence of Staphylococcus aureus:
RT   identification and characterization of genes involved in production of a
RT   siderophore.";
RL   Infect. Immun. 72:29-37(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX   PubMed=19775248; DOI=10.1111/j.1365-2958.2009.06880.x;
RA   Cheung J., Beasley F.C., Liu S., Lajoie G.A., Heinrichs D.E.;
RT   "Molecular characterization of staphyloferrin B biosynthesis in
RT   Staphylococcus aureus.";
RL   Mol. Microbiol. 74:594-608(2009).
CC   -!- FUNCTION: Catalyzes the condensation of L-2,3-diaminopropionic acid (L-
CC       Dap) and citryl-diaminoethane to form L-2,3-diaminopropionyl-citryl-
CC       diaminoethane, the third step in staphyloferrin B biosynthesis.
CC       {ECO:0000269|PubMed:19775248}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-diaminopropanoate + 2-[(2-aminoethylcarbamoyl)methyl]-
CC         2-hydroxybutanedioate + ATP = 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-
CC         (2-aminoethylcarbamoyl)-2-hydroxypropanoate + AMP + diphosphate;
CC         Xref=Rhea:RHEA:59128, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57721, ChEBI:CHEBI:142970, ChEBI:CHEBI:142971,
CC         ChEBI:CHEBI:456215; EC=6.3.2.55;
CC         Evidence={ECO:0000269|PubMed:19775248};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59129;
CC         Evidence={ECO:0000269|PubMed:19775248};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:19775248}.
CC   -!- SUBUNIT: Forms a mixture of monomer and dimer in solution.
CC       {ECO:0000269|PubMed:19775248}.
CC   -!- INDUCTION: Up-regulated under iron-deficient growth conditions.
CC       Repressed by Fur under iron-rich growth conditions.
CC       {ECO:0000269|PubMed:14688077}.
CC   -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP82068.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY251022; AAP82068.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000253; ABD29263.1; -; Genomic_DNA.
DR   RefSeq; WP_001795559.1; NZ_LS483365.1.
DR   RefSeq; YP_498680.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1M8; -.
DR   SMR; Q2G1M8; -.
DR   STRING; 1280.SAXN108_0107; -.
DR   EnsemblBacteria; ABD29263; ABD29263; SAOUHSC_00080.
DR   GeneID; 3919458; -.
DR   KEGG; sao:SAOUHSC_00080; -.
DR   PATRIC; fig|93061.5.peg.69; -.
DR   eggNOG; COG4264; Bacteria.
DR   HOGENOM; CLU_018524_0_1_9; -.
DR   OMA; HPWQWWN; -.
DR   BioCyc; MetaCyc:G1I0R-74-MON; -.
DR   BRENDA; 6.3.2.55; 3352.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR007310; Aerobactin_biosyn_IucA/IucC_N.
DR   InterPro; IPR022770; FhuF_domain.
DR   InterPro; IPR037455; LucA/IucC-like.
DR   PANTHER; PTHR34384; PTHR34384; 1.
DR   Pfam; PF06276; FhuF; 1.
DR   Pfam; PF04183; IucA_IucC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..616
FT                   /note="2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-
FT                   aminoethylcarbamoyl)-2-hydroxypropanoate synthase"
FT                   /id="PRO_0000447127"
SQ   SEQUENCE   616 AA;  71952 MW;  550E3543A64A9090 CRC64;
     MIVVQTLFIH IYQIQFVITR RYRIVNQTIL NRVKTRVMHQ LVSSLIYENI VVYKASYQDG
     VGHFTIEGHD SEYRFTAEKT HSFDRIRITS PIERVVGDEA DTTTDYTQLL REVVFTFPKN
     DEKLEQFIVE LLQTELKDTQ SMQYRESNPP ATPETFNDYE FYAMEGHQYH PSYKSRLGFT
     LSDNLKFGPD FVPNVKLQWL AIDKDKVETT VSRNVVVNEM LRQQVGDKTY EHFVQQIEAS
     GKHVNDVEMI PVHPWQFEHV IQVDLAEERL NGTVLWLGES DELYHPQQSI RTMSPIDTTK
     YYLKVPISIT NTSTKRVLAP HTIENAAQIT DWLKQIQQQD MYLKDELKTV FLGEVLGQSY
     LNTQLSPYKQ TQVYGALGVI WRENIYHMLI DEEDAIPFNA LYASDKDGVP FIENWIKQYG
     SEAWTKQFLA VAIRPMIHML YYHGIAFESH AQNMMLIHEN GWPTRIALKD FHDGVRFKRE
     HLSEAASHLT LKPMPEAHKK VNSNSFIETD DERLVRDFLH DAFFFINIAE IILFIEKQYG
     IDEELQWQWV KGIIEAYQEA FPELNNYQHF DLFEPTIQVE KLTTRRLLSD SELRIHHVTN
     PLGVGGINDA TTISET