ID A0A1I6BT68_9BACI Unreviewed; 459 AA.
AC A0A1I6BT68;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488577_2329 {ECO:0000313|EMBL:SFQ84129.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ84129.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ84129.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ84129.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOYF01000003; SFQ84129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6BT68; -.
DR STRING; 1761761.SAMN04488577_2329; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000199578; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFQ84129.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199578};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..237
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 245..459
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 459 AA; 52333 MW; C6FC54AF311FBB6E CRC64;
MKSLYVKFVV VTIGIMFLSG ILAFFISNTY YQQKLKPFND QKNTKIALDI AVFVENHPDV
NLNEYLENIS AIGYQIYLVD PLGKESYFGA PFRDNSLPSS TKQYVLNGDI YHGILHFPEH
TFVTGFFANE LKNSIGIPLT HNGKDFALFL RPDIKLLFNE MHLLFGWLLT LAITLSIVMV
VFSTKYLVKP ISRLTNATKS LANGNFNVVL DINRRDELGE LSHSFLQMAK KLEQMDEMRK
EFISNISHDI QSPLSNIKGY TNLLDNESMS LEERSQYVSI INGEIKRLST LTKQLLLLAS
LDRNNELMVK KRFNVDQQIK ELIRNYQWLI SEKEIMISYT LPETSILGDP SLLNTIWDNL
LSNAIKYNKP QGNIDISIVE SKESIKVTFK DTGIGLDKTE LGRIFERFYR ADRARTRTIE
GTGLGLSIVD TIVKLHDGNI IVHSKAEEGT TFVVELPVR
//