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Database: UniProt
Entry: R6SDF0_9FIRM
LinkDB: R6SDF0_9FIRM
Original site: R6SDF0_9FIRM 
ID   R6SDF0_9FIRM            Unreviewed;       364 AA.
AC   R6SDF0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BN586_00031 {ECO:0000313|EMBL:CDC59203.1};
OS   Dorea formicigenerans CAG:28.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC59203.1, ECO:0000313|Proteomes:UP000018109};
RN   [1] {ECO:0000313|EMBL:CDC59203.1, ECO:0000313|Proteomes:UP000018109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDC59203.1}.
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DR   EMBL; CBFN010000204; CDC59203.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6SDF0; -.
DR   Proteomes; UP000018109; 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; 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, ECO:0000313|EMBL:CDC59203.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018109};
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        72..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          96..145
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          153..364
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   364 AA;  40823 MW;  264E55FDDC352FA1 CRC64;
     MKYMEIKIMM KYFTHTNAGK LKLNFRAKMN LLTTGLIFVL LLLSTFLGNG VMILLIHHGF
     INAGPPSSQI PLLIQTGIIS IIIGTLITLL ISHLPLKPLH TLVEAIHQVS TGNYDVKIHL
     EHPAEFREVS DCFNHMTEEL SCTEMLRSDF INNFSHEFKT PIVSVLGFAK LLKSDQLTKD
     QREEYLDIII EESRRLSELS TTILDLSRIE SLSSLSGQTT FSLSEQIREA ILLLEYKWSQ
     KHLKLDLNLE ELDILADEAL LKQVWINLLD NGIKFSPEFG KLSVSLHTKD GTCIVKVQDH
     GPGMDQATSD LIFTKFYQGD TSHQSEGNGL GLALVKKIIE LHRGTVTVES NTGKGSTFIV
     VLPL
//
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