SBNC_STAA8
ID SBNC_STAA8 Reviewed; 584 AA.
AC Q2G1N1; Q6X7U5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Staphyloferrin B synthase {ECO:0000305};
DE EC=6.3.2.56 {ECO:0000269|PubMed:19775248};
DE AltName: Full=Staphyloferrin B biosynthesis protein SbnC {ECO:0000305};
GN Name=sbnC {ECO:0000303|PubMed:14688077};
GN OrderedLocusNames=SAOUHSC_00077 {ECO:0000312|EMBL:ABD29260.1};
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-diaminopropionyl-citryl-
CC diaminoethane and 2-oxoglutarate to form staphyloferrin B, the fourth
CC and last step in staphyloferrin B biosynthesis.
CC {ECO:0000269|PubMed:19775248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-
CC 2-hydroxypropanoate + 2-oxoglutarate + ATP = AMP + diphosphate + H(+)
CC + staphyloferrin B; Xref=Rhea:RHEA:59132, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:136993, ChEBI:CHEBI:142971, ChEBI:CHEBI:456215;
CC EC=6.3.2.56; Evidence={ECO:0000269|PubMed:19775248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59133;
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}.
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DR EMBL; AY251022; AAP82065.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29260.1; -; Genomic_DNA.
DR RefSeq; WP_001179384.1; NZ_LS483365.1.
DR RefSeq; YP_498677.1; NC_007795.1.
DR PDB; 7CBB; X-ray; 2.60 A; A/B=1-584.
DR PDBsum; 7CBB; -.
DR AlphaFoldDB; Q2G1N1; -.
DR SMR; Q2G1N1; -.
DR STRING; 1280.SAXN108_0104; -.
DR EnsemblBacteria; ABD29260; ABD29260; SAOUHSC_00077.
DR EnsemblBacteria; KXA40236; KXA40236; HMPREF3211_00221.
DR EnsemblBacteria; SUL22162; SUL22162; NCTC10654_00148.
DR EnsemblBacteria; SUL30543; SUL30543; NCTC10702_00266.
DR GeneID; 3919455; -.
DR KEGG; sao:SAOUHSC_00077; -.
DR PATRIC; fig|1280.3350.peg.96; -.
DR eggNOG; COG4264; Bacteria.
DR HOGENOM; CLU_030178_0_0_9; -.
DR OMA; RLPVKAM; -.
DR BioCyc; MetaCyc:G1I0R-71-MON; -.
DR BRENDA; 6.3.2.56; 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 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..584
FT /note="Staphyloferrin B synthase"
FT /id="PRO_0000447125"
FT HELIX 4..25
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 107..126
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 249..262
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 296..315
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 317..322
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 393..415
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 452..457
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 480..490
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 495..507
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 511..528
FT /evidence="ECO:0007829|PDB:7CBB"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 536..543
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:7CBB"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:7CBB"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:7CBB"
SQ SEQUENCE 584 AA; 66433 MW; E4AF5D127E05F0C7 CRC64;
MQNHTAVNTA QAIILRDLVD ALLFEDIAGI VSNSEITKEN GQTLLIYERE TQQIKIPVYF
SALNMFRYES SQPITIEGRV SKQPLTAAEF WQTIANMNCD LSHEWEVARV EEGLTTAATQ
LAKQLSELDL ASHPFVMSEQ FASLKDRPFH PLAKEKRGLR EADYQVYQAE LNQSFPLMVA
AVKKTHMIHG DTANIDELEN LTVPIKEQAT DMLNDQGLSI DDYVLFPVHP WQYQHILPNV
FAKEISEKLV VLLPLKFGDY LSSSSMRSLI DIGAPYNHVK VPFAMQSLGA LRLTPTRYMK
NGEQAEQLLR QLIEKDEALA KYVMVCDETA WWSYMGQDND IFKDQLGHLT VQLRKYPEVL
AKNDTQQLVS MAALAANDRT LYQMICGKDN ISKNDVMTLF EDIAQVFLKV TLSFMQYGAL
PELHGQNILL SFEDGRVQKC VLRDHDTVRI YKPWLTAHQL SLPKYVVRED TPNTLINEDL
ETFFAYFQTL AVSVNLYAII DAIQDLFGVS EHELMSLLKQ ILKNEVATIS WVTTDQLAVR
HILFDKQTWP FKQILLPLLY QRDSGGGSMP SGLTTVPNPM VTYD
