ID A0A1L8TQ56_9ENTE Unreviewed; 316 AA.
AC A0A1L8TQ56;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RV04_GL001428 {ECO:0000313|EMBL:OJG46262.1};
OS Enterococcus hermanniensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=249189 {ECO:0000313|EMBL:OJG46262.1, ECO:0000313|Proteomes:UP000182077};
RN [1] {ECO:0000313|EMBL:OJG46262.1, ECO:0000313|Proteomes:UP000182077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17122 {ECO:0000313|EMBL:OJG46262.1,
RC ECO:0000313|Proteomes:UP000182077};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG46262.1}.
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DR EMBL; JXKQ01000003; OJG46262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8TQ56; -.
DR STRING; 249189.RV04_GL001428; -.
DR Proteomes; UP000182077; 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; 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; 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; 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:OJG46262.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000182077};
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 26..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..97
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 105..316
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 316 AA; 35887 MW; 200EAB0E9052883B CRC64;
MAIQWNAFFQ NYILNNRKKY YPEKELGASY LIIIVLIIVF YFVSKKSFQY TTKITDGIND
VANGDYTVKL DVAEGGPYKD VFKNFNKMTD ELNSVTTLKS DFINNFSHEF KTPIASIQGF
AELLLKTDIP EDDKNNYLKI IANESARLSE LSNNIMLLTS LESQEIVVEM QSYALEEQLK
QVIILLMPQL THKNIAINVD LVPMAYYGNK SMMQQLWTNI LTNSIKFTPE NGAISVSSKV
VREKYIVSFK DSGIGMDEET KNKIFDKFYQ KQKNSEAKGL GLGLSIVKRI LELIDGEVTV
SSSPEKGSTF IFSIKC
//
