ID   SFNAD_STAA8             Reviewed;         658 AA.
AC   Q2FW70;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=D-ornithine--citrate ligase {ECO:0000305};
DE            EC=6.3.2.58 {ECO:0000269|PubMed:19138128};
GN   Name=sfnaD {ECO:0000303|PubMed:19138128};
GN   OrderedLocusNames=SAOUHSC_02436 {ECO:0000312|EMBL:ABD31458.1};
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 [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   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=RN4220;
RX   PubMed=19138128; DOI=10.1021/bi801844c;
RA   Cotton J.L., Tao J., Balibar C.J.;
RT   "Identification and characterization of the Staphylococcus aureus gene
RT   cluster coding for staphyloferrin A.";
RL   Biochemistry 48:1025-1035(2009).
CC   -!- FUNCTION: Involved in the biosynthesis of the siderophore
CC       staphyloferrin A. Catalyzes the ATP-dependent condensation of D-
CC       ornithine and citrate to form a citryl-D-ornithine intermediate.
CC       {ECO:0000269|PubMed:19138128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + citrate + D-ornithine = AMP + diphosphate + H(+) + N(5)-
CC         [(S)-citryl]-D-ornithine; Xref=Rhea:RHEA:59136, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16947, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57668, ChEBI:CHEBI:142972, ChEBI:CHEBI:456215;
CC         EC=6.3.2.58; Evidence={ECO:0000269|PubMed:19138128};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59137;
CC         Evidence={ECO:0000269|PubMed:19138128};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:19138128}.
CC   -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
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DR   EMBL; CP000253; ABD31458.1; -; Genomic_DNA.
DR   RefSeq; WP_001052567.1; NZ_LS483365.1.
DR   RefSeq; YP_500905.1; NC_007795.1.
DR   AlphaFoldDB; Q2FW70; -.
DR   SMR; Q2FW70; -.
DR   STRING; 1280.SAXN108_2429; -.
DR   EnsemblBacteria; ABD31458; ABD31458; SAOUHSC_02436.
DR   GeneID; 3919001; -.
DR   KEGG; sao:SAOUHSC_02436; -.
DR   PATRIC; fig|93061.5.peg.2197; -.
DR   eggNOG; COG4264; Bacteria.
DR   HOGENOM; CLU_018524_3_1_9; -.
DR   OMA; ELCHCFF; -.
DR   BioCyc; MetaCyc:MON-20492; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
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..658
FT                   /note="D-ornithine--citrate ligase"
FT                   /id="PRO_0000453635"
SQ   SEQUENCE   658 AA;  76087 MW;  B3442E03671368E6 CRC64;
     MNLNLIFKEQ TLKFNKEEQE TYLFLQQHNS DWANIFKEMI LQGRDKVTQR LVTSMHRENL
     VKARTQSKKI LSRDLIMLDI STTHILEIQF PQAKQTLYAP ITGEHAFDRI DVEGPFYIKD
     DITNTITRVH HPNEILECIL IEAPDLKNAA SDQFQQDLIN SATNMTFAIS YQALSMQHDS
     APLFNIIENS EDSYLRSEQA VIEGHPLHPG AKLRKGLNAL QTFLYSSEFN QPIKLKIVLI
     HSKLSRTMSL SKDYDTTVHQ LFPDLIKQLE NEFTPKFNFN DYHIMIVHPW QLDDVLHSDY
     QAEVDKELII EAKHTLDYYA GLSFRTLVPK YPAMSPHIKL STNVHITGEI RTLSEQTTHN
     GPLMTRILND ILEKDVIFKS YASTIIDEVA GIHFYNEQDE ADYQTERSEQ LGTLFRKNIY
     QMIPQEVTPL IPSSLVATYP FNNESPIVTL IKRYQSAASL SDFESSAKSW VETYSKALLG
     LVIPLVTKYG IALEAHLQNA IATFRKDGLL DTMYIRDFEG LRIDKAQLNE MVYSTSHFHE
     KSRILTDSKT SVFNKAFYST VQNHLGELIL TISKASNDSN LERHMWYIVR DVLDNIFDQL
     VLSTHKSNQV NENRINEIKD TMFAPFIDYK CVTTMRLEDE AHHYTYIKVN NPLYRENN