ID   SBNE_STAA8              Reviewed;         578 AA.
AC   Q2G1M9; Q6X7U3;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=L-2,3-diaminopropanoate--citrate ligase {ECO:0000305};
DE            EC=6.3.2.54 {ECO:0000269|PubMed:19775248};
DE   AltName: Full=Staphyloferrin B biosynthesis protein SbnE {ECO:0000305};
GN   Name=sbnE {ECO:0000303|PubMed:14688077};
GN   OrderedLocusNames=SAOUHSC_00079 {ECO:0000312|EMBL:ABD29262.1};
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], PATHWAY, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   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 synthesis of citryl-L-2,3-diaminopropionic acid
CC       from L-2,3-diaminopropionic acid (L-Dap) and citrate, the first step in
CC       staphyloferrin B biosynthesis. {ECO:0000269|PubMed:19775248}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-diaminopropanoate + ATP + citrate = 2-[(L-alanin-3-
CC         ylcarbamoyl)methyl]-2-hydroxybutanedioate + AMP + diphosphate;
CC         Xref=Rhea:RHEA:59124, ChEBI:CHEBI:16947, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57721, ChEBI:CHEBI:142969,
CC         ChEBI:CHEBI:456215; EC=6.3.2.54;
CC         Evidence={ECO:0000269|PubMed:19775248};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59125;
CC         Evidence={ECO:0000269|PubMed:19775248};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.99 mM for citrate {ECO:0000269|PubMed:19775248};
CC         Note=kcat is 16.08 min(-1) with citrate as substrate.
CC         {ECO:0000269|PubMed:19775248};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:14688077,
CC       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   -!- DISRUPTION PHENOTYPE: Mutant shows a growth defect in iron-deficient
CC       medium and is significantly attenuated in a murine kidney abscess model
CC       of infection. {ECO:0000269|PubMed:14688077}.
CC   -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
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DR   EMBL; AY251022; AAP82067.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD29262.1; -; Genomic_DNA.
DR   RefSeq; WP_001179888.1; NZ_LS483365.1.
DR   RefSeq; YP_498679.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1M9; -.
DR   SMR; Q2G1M9; -.
DR   STRING; 1280.SAXN108_0106; -.
DR   EnsemblBacteria; ABD29262; ABD29262; SAOUHSC_00079.
DR   EnsemblBacteria; KXA40238; KXA40238; HMPREF3211_00223.
DR   EnsemblBacteria; SUL22234; SUL22234; NCTC10654_00150.
DR   EnsemblBacteria; SUL30545; SUL30545; NCTC10702_00268.
DR   GeneID; 3919457; -.
DR   KEGG; sao:SAOUHSC_00079; -.
DR   PATRIC; fig|1280.10758.peg.93; -.
DR   eggNOG; COG4264; Bacteria.
DR   HOGENOM; CLU_018283_0_0_9; -.
DR   OMA; TGWHRFG; -.
DR   BioCyc; MetaCyc:G1I0R-73-MON; -.
DR   BRENDA; 6.3.2.54; 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..578
FT                   /note="L-2,3-diaminopropanoate--citrate ligase"
FT                   /id="PRO_0000447126"
SQ   SEQUENCE   578 AA;  65999 MW;  38CA6B8BC41432AB CRC64;
     MQNKELIQHA AYAAIERILN EYFREENLYQ VPPQNHQWSI QLSELETLTG EFRYWSAMGH
     HMYHPEVWLI DGKSKKITTY KEAIARILQH MAQSADNQTA VQQHMAQIMS DIDNSIHRTA
     RYLQSNTIDY VEDRYIVSEQ SLYLGHPFHP TPKSASGFSE ADLEKYAPEC HTSFQLHYLA
     VHQDVLLTRY VEGKEDQVEK VLYQLADIDI SEIPKDFILL PTHPYQINVL RQHPQYMQYS
     EQGLIKDLGV SGDSVYPTSS VRTVFSKALN IYLKLPIHVK ITNFIRTNDL EQIERTIDAA
     QVIASVKDEV ETPHFKLMFE EGYRALLPNP LGQTVEPEMD LLTNSAMIVR EGIPNYHADK
     DIHVLASLFE TMPDSPMSKL SQVIEQSGLA PEAWLECYLN RTLLPILKLF SNTGISLEAH
     VQNTLIELKD GIPDVCFVRD LEGICLSRTI ATEKQLVPNV VAASSPVVYA HDEAWHRLKY
     YVVVNHLGHL VSTIGKATRN EVVLWQLVAH RLMTWKKEYA NNAVFVDCVE DLYQTPTIAA
     KANLMSKLND CGANPIYTHI PNPICHNKEV SYCESNNS