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Database: UniProt
Entry: L5NEU1_9BACI
LinkDB: L5NEU1_9BACI
Original site: L5NEU1_9BACI 
ID   L5NEU1_9BACI            Unreviewed;       457 AA.
AC   L5NEU1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=D479_02127 {ECO:0000313|EMBL:ELK48618.1};
OS   Halobacillus sp. BAB-2008.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK48618.1, ECO:0000313|Proteomes:UP000010769};
RN   [1] {ECO:0000313|EMBL:ELK48618.1, ECO:0000313|Proteomes:UP000010769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK48618.1,
RC   ECO:0000313|Proteomes:UP000010769};
RX   PubMed=23469348;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT   BAB-2008.";
RL   Genome Announc. 1:E00222-12(2013).
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}.
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:ELK48618.1}.
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DR   EMBL; ANPF01000005; ELK48618.1; -; Genomic_DNA.
DR   RefSeq; WP_008633094.1; NZ_ANPF01000005.1.
DR   AlphaFoldDB; L5NEU1; -.
DR   PATRIC; fig|1246484.3.peg.443; -.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000010769; 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; 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:ELK48618.1};
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:UP000010769};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          183..235
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          243..457
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   457 AA;  51579 MW;  5804F7849D0EA83F CRC64;
     MKTLYSKFLW TTLFIMIGSA VTGFLLSNLY YQNELKPEND TKNTKIALQM AAYGETEKSL
     EDFLEHTAST GYQLYLFSEK EGKQYFGRSF NEHNLPASAV SRVIEGDIYH GMRDFPKETF
     VTGFFANELR NTVGVPLTYE GTRYALFMRP DIELLFNELH ILLAWMVAAI VLLSLAAMLI
     WSGLIIHPIR KLTAAVNKVG EEGFGVYLKV TRKDEIGQLA RRFNDMITRL GKLDEMRKSF
     VSNVSHDIRT PLSNIQGYSR LLENDNLPHA ERQKYLAVIQ EEAERMSALS SQLLTLSSLS
     PEEENIKKSP VDVSGQLKQL IRRYHWRIDE AGMSISYNLD EMICLGNEAL LYTVWENLLT
     NAIKYNSTEG TISIQGTATA DEINVSITDC GIGLSEEEQE QVFDRFYRAD QARSRSVPGT
     GLGLSIVKEI IDLHDGSVHL HSEPGSGSTF LVTLPRL
//
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