ID   SFNAB_STAA8             Reviewed;         585 AA.
AC   Q2FW72;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Staphyloferrin A synthase {ECO:0000305};
DE            EC=6.3.2.57 {ECO:0000269|PubMed:19138128};
GN   Name=sfnaB {ECO:0000303|PubMed:19138128};
GN   OrderedLocusNames=SAOUHSC_02434 {ECO:0000312|EMBL:ABD31456.1};
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 a citryl-
CC       D-ornithine intermediate, produced by SfnaD, and citrate to form
CC       staphyloferrin A. {ECO:0000269|PubMed:19138128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + citrate + N(5)-[(S)-citryl]-D-ornithine = AMP +
CC         diphosphate + H(+) + staphyloferrin A; Xref=Rhea:RHEA:59140,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16947, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:142972, ChEBI:CHEBI:142973,
CC         ChEBI:CHEBI:456215; EC=6.3.2.57;
CC         Evidence={ECO:0000269|PubMed:19138128};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59141;
CC         Evidence={ECO:0000269|PubMed:19138128};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:19138128}.
CC   -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000253; ABD31456.1; -; Genomic_DNA.
DR   RefSeq; WP_000262640.1; NZ_LS483365.1.
DR   RefSeq; YP_500903.1; NC_007795.1.
DR   AlphaFoldDB; Q2FW72; -.
DR   SMR; Q2FW72; -.
DR   STRING; 1280.SAXN108_2426; -.
DR   EnsemblBacteria; ABD31456; ABD31456; SAOUHSC_02434.
DR   GeneID; 3918999; -.
DR   KEGG; sao:SAOUHSC_02434; -.
DR   PATRIC; fig|93061.5.peg.2195; -.
DR   eggNOG; COG4264; Bacteria.
DR   HOGENOM; CLU_018524_3_1_9; -.
DR   OMA; THPMHKT; -.
DR   BioCyc; MetaCyc:MON-20491; -.
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..585
FT                   /note="Staphyloferrin A synthase"
FT                   /id="PRO_0000453634"
SQ   SEQUENCE   585 AA;  67211 MW;  CDEE894C6340D82B CRC64;
     MVYLEWAKAD RNIQYRVINA IIKERIYPEQ TFISQKGSLI EIQYHMHVLT IEVVRKSALE
     RYEFTGDITY LNKGETSLII TLEGLLDVLN HDFDIPISER LREELIHSRD SLVETYKQMS
     HRQTLISQSF KFSRLPQDIN FFSWLQHVKD SDKTDDLTYS ESLVPEGHPT HPLTKTKLPL
     TMEEVRAYAP EFEKEIPLQI MMIEKDHVVC TAMDGNDQFI IDEIIPEYYN QIRVFLKSLG
     LKSEDYRAIL VHPWQYDHTI GKYFEAWIAK KILIPTPFTI LSKATLSFRT MSLIDKPYHV
     KLPVDAQATS AVRTVSTVTT VDGPKLSYAL QNMLNQYPGF KVAMEPFGEY ANVDKDRARQ
     LACIIRQKPE IDGKGATVVS ASLVNKNPID QKVIVDSYLE WLNQGITKES ITTFIERYAQ
     ALIPPLIAFI QNYGIALEAH MQNTVVNLGP HFDIQFLVRD LGGSRIDLET LQHRVSDIKI
     TNDSLIADSI DAVIAKFQHA VIQNQMAELI HHFNQYDCVE ETELFNIVQQ VVAHAINPTL
     PHANELKDIL FGPTITVKAL LNMRMENKVK QYLNIELDNP IKKEV