SBNI_STAA8
ID SBNI_STAA8 Reviewed; 254 AA.
AC Q2G1M5; Q6X7T9;
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=L-serine kinase SbnI {ECO:0000305};
DE EC=2.7.1.225 {ECO:0000269|PubMed:29483190};
DE AltName: Full=Staphyloferrin B biosynthesis regulatory protein SbnI {ECO:0000305};
GN Name=sbnI {ECO:0000303|PubMed:14688077};
GN OrderedLocusNames=SAOUHSC_00083 {ECO:0000312|EMBL:ABD29266.1};
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, ACTIVITY REGULATION, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=26534960; DOI=10.1074/jbc.m115.696625;
RA Laakso H.A., Marolda C.L., Pinter T.B., Stillman M.J., Heinrichs D.E.;
RT "A heme-responsive regulator controls synthesis of staphyloferrin B in
RT Staphylococcus aureus.";
RL J. Biol. Chem. 291:29-40(2016).
RN [4] {ECO:0007744|PDB:5UJE}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-240, FUNCTION AS A KINASE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT,
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-20 AND ASP-58, AND ACTIVE SITE.
RX PubMed=29483190; DOI=10.1074/jbc.ra118.001875;
RA Verstraete M.M., Perez-Borrajero C., Brown K.L., Heinrichs D.E.,
RA Murphy M.E.P.;
RT "SbnI is a free serine kinase that generates O-phospho-L-serine for
RT staphyloferrin B biosynthesis in Staphylococcus aureus.";
RL J. Biol. Chem. 293:6147-6160(2018).
CC -!- FUNCTION: Free serine kinase that uses ATP to phosphorylate L-serine to
CC yield O-phospho-L-serine and ADP. O-phospho-L-serine serves as a
CC substrate for SbnA and is a precursor for staphyloferrin B biosynthesis
CC (PubMed:29483190). Is also a DNA-binding regulatory protein that senses
CC heme to control gene expression for siderophore biosynthesis. Binds to
CC DNA within the sbnC coding region and is required for expression of
CC genes in the sbn operon from sbnD onward (PubMed:26534960).
CC {ECO:0000269|PubMed:26534960, ECO:0000269|PubMed:29483190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine = ADP + H(+) + O-phospho-L-serine;
CC Xref=Rhea:RHEA:59112, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57524, ChEBI:CHEBI:456216;
CC EC=2.7.1.225; Evidence={ECO:0000269|PubMed:29483190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59113;
CC Evidence={ECO:0000269|PubMed:29483190};
CC -!- ACTIVITY REGULATION: Binds heme and heme binding inhibits DNA binding.
CC {ECO:0000269|PubMed:26534960}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for ATP {ECO:0000269|PubMed:29483190};
CC KM=340 mM for L-serine {ECO:0000269|PubMed:29483190};
CC Note=kcat is 3.9 min(-1) with ATP as substrate. kcat is 14.3 min(-1)
CC with L-serine as substrate. {ECO:0000269|PubMed:29483190};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:26534960,
CC ECO:0000269|PubMed:29483190}.
CC -!- SUBUNIT: Forms dimers and tetramers in solution (PubMed:26534960).
CC Predominantly forms dimers (PubMed:29483190).
CC Dimerization/oligomerization is not essential for kinase activity
CC (PubMed:29483190). {ECO:0000269|PubMed:26534960,
CC ECO:0000269|PubMed:29483190}.
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 is impaired for staphyloferrin B
CC production. {ECO:0000269|PubMed:26534960, ECO:0000269|PubMed:29483190}.
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DR EMBL; AY251022; AAP82071.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29266.1; -; Genomic_DNA.
DR RefSeq; WP_001015549.1; NZ_LS483365.1.
DR RefSeq; YP_498683.1; NC_007795.1.
DR PDB; 5UJE; X-ray; 2.50 A; A=1-240.
DR PDBsum; 5UJE; -.
DR AlphaFoldDB; Q2G1M5; -.
DR SMR; Q2G1M5; -.
DR STRING; 1280.SAXN108_0111; -.
DR EnsemblBacteria; ABD29266; ABD29266; SAOUHSC_00083.
DR EnsemblBacteria; CRI17580; CRI17580; BN1321_40048.
DR EnsemblBacteria; CXN34847; CXN34847; ERS072840_00567.
DR EnsemblBacteria; GBV19671; GBV19671; M1K003_0644.
DR EnsemblBacteria; KXA40242; KXA40242; HMPREF3211_00227.
DR EnsemblBacteria; PPJ75755; PPJ75755; CV021_04050.
DR EnsemblBacteria; PPJ93931; PPJ93931; CSC83_08555.
DR EnsemblBacteria; PPK15801; PPK15801; CSC87_03770.
DR EnsemblBacteria; SCT50441; SCT50441; SAMEA1708674_03227.
DR EnsemblBacteria; SUK38285; SUK38285; NCTC5664_00814.
DR EnsemblBacteria; SUL22238; SUL22238; NCTC10654_00154.
DR EnsemblBacteria; SUL30550; SUL30550; NCTC10702_00273.
DR GeneID; 3919461; -.
DR KEGG; sao:SAOUHSC_00083; -.
DR PATRIC; fig|1280.10341.peg.120; -.
DR eggNOG; COG1475; Bacteria.
DR HOGENOM; CLU_095982_0_0_9; -.
DR OMA; FNIAGRC; -.
DR BioCyc; MetaCyc:G1I0R-77-MON; -.
DR BRENDA; 2.7.1.225; 3352.
DR SABIO-RK; Q2G1M5; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045881; P:positive regulation of sporulation resulting in formation of a cellular spore; IBA:GO_Central.
DR GO; GO:0019290; P:siderophore biosynthetic process; IDA:UniProtKB.
DR CDD; cd16388; SbnI_like_N; 1.
DR Gene3D; 3.30.1760.10; -; 1.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR016999; SbnI-like.
DR InterPro; IPR037953; SbnI-like_N.
DR InterPro; IPR023098; SerK/SbnI_C.
DR Pfam; PF02195; ParBc; 1.
DR PIRSF; PIRSF032543; UCP032543_ParB-like; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..254
FT /note="L-serine kinase SbnI"
FT /id="PRO_0000447121"
FT ACT_SITE 20
FT /evidence="ECO:0000305|PubMed:29483190"
FT BINDING 33
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q5JD03"
FT BINDING 57..61
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:Q5JD03"
FT BINDING 58..62
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q5JD03"
FT BINDING 98
FT /ligand="O-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57524"
FT /evidence="ECO:0000250|UniProtKB:Q5JD03"
FT MUTAGEN 20
FT /note="E->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:29483190"
FT MUTAGEN 58
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:29483190"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:5UJE"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5UJE"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5UJE"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:5UJE"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5UJE"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:5UJE"
SQ SEQUENCE 254 AA; 29633 MW; 587F7937447685E4 CRC64;
MNHIHEHLKL VPVDKIDLHE TFEPLRLEKT KSSIEADDFI RHPILVTAMQ HGRYMVIDGV
HRYTSLKALG CKKVPVQEIH ETQYSISTWQ HKVPFGVWWE TLQQEHRLPW TTETRQEAPF
ITMCHGDTEQ YLYTKDLGEA HFQVWEKVVA SYSGCCSVER IAQGTYPCLS QQDVLMKYQP
LSYKEIEAVV HKGETVPAGV TRFNISGRCL NLQVPLALLK QDDDVEQLRN WKQFLADKFA
NMRCYTEKVY LVEQ
