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Database: UniProt
Entry: R9LS44_9FIRM
LinkDB: R9LS44_9FIRM
Original site: R9LS44_9FIRM 
ID   R9LS44_9FIRM            Unreviewed;       436 AA.
AC   R9LS44;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=C814_01551 {ECO:0000313|EMBL:EOS61629.1};
OS   Anaerotruncus sp. G3(2012).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS61629.1, ECO:0000313|Proteomes:UP000014129};
RN   [1] {ECO:0000313|EMBL:EOS61629.1, ECO:0000313|Proteomes:UP000014129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anaerotruncus bacterium G3.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system HssS/HssR
CC       involved in intracellular heme homeostasis and tempering of
CC       staphylococcal virulence. HssS functions as a heme sensor histidine
CC       kinase which is autophosphorylated at a histidine residue and transfers
CC       its phosphate group to an aspartate residue of HssR. HssR/HssS
CC       activates the expression of hrtAB, an efflux pump, in response to
CC       extracellular heme, hemin, hemoglobin or blood.
CC       {ECO:0000256|ARBA:ARBA00037219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOS61629.1}.
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DR   EMBL; ASTA01000031; EOS61629.1; -; Genomic_DNA.
DR   RefSeq; WP_016316240.1; NZ_KE159674.1.
DR   AlphaFoldDB; R9LS44; -.
DR   STRING; 1235835.C814_01551; -.
DR   PATRIC; fig|1235835.3.peg.1632; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000014129; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45528:SF11; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014129};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   TRANSMEM        148..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          167..220
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          228..436
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   436 AA;  48953 MW;  3C276B63AB88DFEF CRC64;
     MKKRCKRRST VYHQVVGLLC LIMLVTTAVP TVMFSHFSRR AFAGDVQNQV LSSIDTVADY
     LEQHHLPLSD IDELLSFERL RLRILDDLSP LELDKEEQRR LAADGYLVFS RTSGNGLPHA
     MLNRYKDSYI LVQADMEPIF RLSRQTKLLS LLLTLLIGLI AAMIGGYRLL VPVRMLDEAT
     RKVAAGDFTV RIPAPKRMDE IGSLIESFNT MTRELGSVEM LRSNFVSDIS HEFKTPLTAI
     EGYAKLLEGD CSPEERREYV GTITDETRRL SVLVANILMI NRLDKGNIPS ERHPVRIDEQ
     IRHALALCEA GWTGKNLELD LELDEIYFAG YESLLMQVWA NLIDNAVKFS PDGGRISLAL
     HQKGGRVVFV ICNDGDNIPE ESRPHLFEQF YKADPSRGGE GNGLGLSIVK RVAELHGGEV
     SVENLPGSGV RFTIFL
//
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