SRRB_STAAC
ID SRRB_STAAC Reviewed; 583 AA.
AC Q5HFT1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sensor protein SrrB;
DE EC=2.7.13.3;
DE AltName: Full=Staphylococcal respiratory response protein B;
GN Name=srrB; OrderedLocusNames=SACOL1534;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16859493; DOI=10.1111/j.1365-2958.2006.05290.x;
RA Richardson A.R., Dunman P.M., Fang F.C.;
RT "The nitrosative stress response of Staphylococcus aureus is required for
RT resistance to innate immunity.";
RL Mol. Microbiol. 61:927-939(2006).
RN [3]
RP INDUCTION DURING ANAEROBIC GROWTH.
RX PubMed=17384184; DOI=10.1128/jb.00081-07;
RA Fuchs S., Pane-Farre J., Kohler C., Hecker M., Engelmann S.;
RT "Anaerobic gene expression in Staphylococcus aureus.";
RL J. Bacteriol. 189:4275-4289(2007).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24222487; DOI=10.1128/mbio.00696-13;
RA Kinkel T.L., Roux C.M., Dunman P.M., Fang F.C.;
RT "The Staphylococcus aureus SrrAB two-component system promotes resistance
RT to nitrosative stress and hypoxia.";
RL MBio 4:E00696-E00713(2013).
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 (PubMed:24222487). Also plays an essential role in host-
CC derived nitric oxide resistance by regulating hmp/flavohemoglobin, an
CC enzyme that detoxifies nitric oxide by converting it to nitrate
CC (PubMed:16859493, PubMed:24222487). 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 (Probable). {ECO:0000269|PubMed:16859493,
CC ECO:0000269|PubMed:24222487, ECO:0000305}.
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 -!- INDUCTION: Up-regulated during anaerobic growth.
CC {ECO:0000269|PubMed:17384184}.
CC -!- DISRUPTION PHENOTYPE: Inactivation significantly enhances
CC staphylococcal nitric oxide susceptibility.
CC {ECO:0000269|PubMed:16859493}.
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DR EMBL; CP000046; AAW36727.1; -; Genomic_DNA.
DR RefSeq; WP_000987769.1; NC_002951.2.
DR AlphaFoldDB; Q5HFT1; -.
DR SMR; Q5HFT1; -.
DR EnsemblBacteria; AAW36727; AAW36727; SACOL1534.
DR KEGG; sac:SACOL1534; -.
DR HOGENOM; CLU_000445_89_2_9; -.
DR OMA; FNQMGRQ; -.
DR Proteomes; UP000000530; 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 2: Evidence at transcript level;
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_0000074882"
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; 66076 MW; 7305F6883B016640 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 NARFFVVTTS 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
