SRRB_STAAU
ID SRRB_STAAU Reviewed; 583 AA.
AC Q9L523; Q6XZ98;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Sensor protein SrrB;
DE EC=2.7.13.3;
DE AltName: Full=Staphylococcal respiratory response protein B;
GN Name=srrB;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=MN8;
RX PubMed=11157922; DOI=10.1128/jb.183.4.1113-1123.2001;
RA Yarwood J.M., McCormick J.K., Schlievert P.M.;
RT "Identification of a novel two-component regulatory system that acts in
RT global regulation of virulence factors of Staphylococcus aureus.";
RL J. Bacteriol. 183:1113-1123(2001).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=MN8;
RX PubMed=15060046; DOI=10.1128/jb.186.8.2430-2438.2004;
RA Pragman A.A., Yarwood J.M., Tripp T.J., Schlievert P.M.;
RT "Characterization of virulence factor regulation by SrrAB, a two-component
RT system in Staphylococcus aureus.";
RL J. Bacteriol. 186:2430-2438(2004).
CC -!- FUNCTION: Member of the two-component regulatory system SrrA/SrrB,
CC which is involved in the global regulation of staphylococcal virulence
CC factors in response to environmental oxygen levels as well as biofilm
CC formation. Also plays an essential role in host-derived nitric oxide
CC resistance by regulating hmp/flavohemoglobin, an enzyme that detoxifies
CC nitric oxide by converting it to nitrate. Functions as a sensor protein
CC kinase which is autophosphorylated at a histidine residue and transfers
CC its phosphate group to SrrA. In turn, SrrA binds to the upstream
CC promoter regions of the target genes to positively and negatively
CC regulate their expression. {ECO:0000250|UniProtKB:Q5HFT1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060046};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15060046}.
CC -!- INDUCTION: Activated by SrrA. Expression is maximal during the
CC postexponential phase of growth, particularly under microaerobic
CC conditions. {ECO:0000269|PubMed:11157922}.
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DR EMBL; AF260326; AAF70313.1; -; Genomic_DNA.
DR RefSeq; WP_043054894.1; NZ_UHBW01000001.1.
DR PDB; 6PAJ; X-ray; 2.00 A; A/B=355-583.
DR PDB; 7JL6; X-ray; 2.10 A; A/B=258-358.
DR PDBsum; 6PAJ; -.
DR PDBsum; 7JL6; -.
DR AlphaFoldDB; Q9L523; -.
DR SMR; Q9L523; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR041328; HisK_sensor.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF18698; HisK_sensor; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..583
FT /note="Sensor protein SrrB"
FT /id="PRO_0000074881"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 197..249
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 366..583
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 369
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:7JL6"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:7JL6"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:7JL6"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:7JL6"
FT HELIX 294..310
FT /evidence="ECO:0007829|PDB:7JL6"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:7JL6"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:7JL6"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:7JL6"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:7JL6"
FT HELIX 357..386
FT /evidence="ECO:0007829|PDB:6PAJ"
FT HELIX 393..425
FT /evidence="ECO:0007829|PDB:6PAJ"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:6PAJ"
FT HELIX 438..447
FT /evidence="ECO:0007829|PDB:6PAJ"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:6PAJ"
FT HELIX 473..488
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 496..503
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 505..514
FT /evidence="ECO:0007829|PDB:6PAJ"
FT HELIX 547..556
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 562..568
FT /evidence="ECO:0007829|PDB:6PAJ"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:6PAJ"
FT STRAND 572..580
FT /evidence="ECO:0007829|PDB:6PAJ"
SQ SEQUENCE 583 AA; 66106 MW; 730EF6383B0617F0 CRC64;
MMSRLNSVVI KLWLTIILIV TTVLILLSIA LITFMQYYFT QETENAIRED ARRISSLVEQ
SHNKEEAIKY SQTLIENPGG LMIINNKHRQ STASLSNIKK QMLNEVVNND HFDDVFDKGK
SVTRNVTIKE KGSSQTYILL GYPTKAQKNS HSKYSGVFIY KDLKSIEDTN NAITIITIIT
AVIFLTITTV FAFFLSSRIT KPLRRLRDQA TRVSEGDYSY KPSVTTKDEI GQLSQAFNQM
STEIEEHVDA LSTSKNIRDS LINSMVEGVL GINESRQIIL SNKMANDIMD NIDEDAKAFL
LRQIEDTFKS KQTEMRDLEM NTRFFVVTTS YIDKIEQGGK SGVVVTVRDM TNEHNLDQMK
KDFIANVSHE LRTPISLLQG YTESIVDGIV TEPDEIKESL AIVLDESKRL NRLVNELLNV
ARMDAEGLSV NKEVQPIAAL LDKMKIKYRQ QADDLGLNMT FNYCKKRVWS YDMDRMDQVL
TNLIDNASRY TKPGDEIAIT CDENESEDIL YIKDTGTGIA PEHLQQVFDR FYKVDAARTR
GKQGTGLGLF ICKMIIEEHG GSIDVKSELG KGTTFIIKLP KPE
