ID A0A1M5RF47_9FIRM Unreviewed; 350 AA.
AC A0A1M5RF47;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02746098_00543 {ECO:0000313|EMBL:SHH24891.1};
OS Desulfosporosinus lacus DSM 15449.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1121420 {ECO:0000313|EMBL:SHH24891.1, ECO:0000313|Proteomes:UP000183954};
RN [1] {ECO:0000313|EMBL:SHH24891.1, ECO:0000313|Proteomes:UP000183954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15449 {ECO:0000313|EMBL:SHH24891.1,
RC ECO:0000313|Proteomes:UP000183954};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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};
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DR EMBL; FQXJ01000003; SHH24891.1; -; Genomic_DNA.
DR RefSeq; WP_073027654.1; NZ_FQXJ01000003.1.
DR AlphaFoldDB; A0A1M5RF47; -.
DR STRING; 1121420.SAMN02746098_00543; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000183954; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SHH24891.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 15..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..129
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 137..350
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 350 AA; 39488 MW; CFF70B2316A44B98 CRC64;
MAKNLSNSIR AKGTLIAIGI LFFSCFVSFS LMTILFLVLY HGDLSISEAH AVFGSFMFVT
LILCVALGGS LLFFAIRKIS DPIIRISNAT KEVAKGDFSI KMDYKSNDEI GVLTQNFNLM
TTELGNMEYL RKDFISSVSH EIKTPIASIQ GFAEMLQDKE LSEENFQAYT NIIIDETKRL
SHLSSNMLRL SKLDHQFIPE ITKQFSLDEQ IRRTIVLLEE KWSKKNLELD IDLEKIVYTG
DEALIQQIWL NLIENAIKFS AESGTVFIHA RKISNKVIAE IKDQGIGISK IDQGRIFEKF
FQVDESHSKE GSGLGLAIVK KIVEIYDGEI DFTSEIGQGT TFVVKLPFRN
//
