ID   HSSR_STAAE              Reviewed;         224 AA.
AC   A6QJK3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Heme response regulator HssR;
GN   Name=hssR; OrderedLocusNames=NWMN_2263;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
RN   [2]
RP   FUNCTION IN REGULATION OF HRTAB EXPRESSION, AND MODULATION OF VIRULENCE.
RX   PubMed=18005689; DOI=10.1016/j.chom.2007.03.001;
RA   Torres V.J., Stauff D.L., Pishchany G., Bezbradica J.S., Gordy L.E.,
RA   Iturregui J., Anderson K.L., Dunman P.M., Joyce S., Skaar E.P.;
RT   "A Staphylococcus aureus regulatory system that responds to host heme and
RT   modulates virulence.";
RL   Cell Host Microbe 1:109-119(2007).
RN   [3]
RP   FUNCTION, REGULATION, PHOSPHORYLATION AT ASP-52, AND MUTAGENESIS OF ASP-52.
RX   PubMed=17635909; DOI=10.1074/jbc.m703797200;
RA   Stauff D.L., Torres V.J., Skaar E.P.;
RT   "Signaling and DNA-binding activities of the Staphylococcus aureus HssR-
RT   HssS two-component system required for heme sensing.";
RL   J. Biol. Chem. 282:26111-26121(2007).
CC   -!- FUNCTION: Member of the two-component regulatory system HssS/HssR
CC       involved in intracellular heme homeostasis and tempering of
CC       staphylococcal virulence. Phosphorylated HssR binds to a direct repeat
CC       sequence within hrtAB promoter and activates the expression of hrtAB,
CC       an efflux pump, in response to extracellular heme, hemin, hemoglobin or
CC       blood. {ECO:0000269|PubMed:17635909, ECO:0000269|PubMed:18005689}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated by HssS. {ECO:0000269|PubMed:17635909}.
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DR   EMBL; AP009351; BAF68535.1; -; Genomic_DNA.
DR   RefSeq; WP_000249491.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QJK3; -.
DR   SMR; A6QJK3; -.
DR   EnsemblBacteria; BAF68535; BAF68535; NWMN_2263.
DR   KEGG; sae:NWMN_2263; -.
DR   HOGENOM; CLU_000445_30_3_9; -.
DR   OMA; WQQSYGD; -.
DR   Proteomes; UP000006386; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; PTHR48111; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system; Virulence.
FT   CHAIN           1..224
FT                   /note="Heme response regulator HssR"
FT                   /id="PRO_0000331330"
FT   DOMAIN          3..116
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        124..222
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         52
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT                   ECO:0000269|PubMed:17635909"
FT   MUTAGEN         52
FT                   /note="D->A: Abolishes phosphorylation by HssS and binding
FT                   to hrtAB promoter."
FT                   /evidence="ECO:0000269|PubMed:17635909"
SQ   SEQUENCE   224 AA;  25958 MW;  30CE2F93940CCC43 CRC64;
     MVQCLVVDDD PRILNYIASH LQIEHIDAYT QPSGEAALKL LEKQRVDIAV VDIMMDGMDG
     FQLCNTLKND YDIPVIMLTA RDALSDKERA FISGTDDYVT KPFEVKELIF RIRAVLRRYN
     INSNSEMTIG NLTLNQSYLE LQVSNKTMTL PNKEFQLLFM LAARPKQIFT REQIIEKIWG
     YDYEGDERTV DVHIKRLRQR LKKLNATLTI ETVRGQGYKV ENHV