SRRB_STAAR
ID SRRB_STAAR Reviewed; 583 AA.
AC Q6GGK7;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
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; OrderedLocusNames=SAR1567;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG40563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571856; CAG40563.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000987777.1; NC_002952.2.
DR AlphaFoldDB; Q6GGK7; -.
DR SMR; Q6GGK7; -.
DR KEGG; sar:SAR1567; -.
DR HOGENOM; CLU_000445_89_2_9; -.
DR OrthoDB; 1827824at2; -.
DR Proteomes; UP000000596; Chromosome.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..583
FT /note="Sensor protein SrrB"
FT /id="PRO_0000074885"
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"
SQ SEQUENCE 583 AA; 66120 MW; 030CA3683B0617F5 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 FNYCKKRVWT YDMDRMDQVL
TNLIDNASRY TKPGDEIAIT CDENESEDIL YIKDTGTGIA PEHLQQVFDR FYKVDAARTR
GKQGTGLGLF ICKMIIEEHG GSIDVKSELG KGTTFIIKLP KPE
