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Database: UniProt
Entry: K6DCA8_9BACI
LinkDB: K6DCA8_9BACI
Original site: K6DCA8_9BACI 
ID   K6DCA8_9BACI            Unreviewed;       457 AA.
AC   K6DCA8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BABA_18097 {ECO:0000313|EMBL:EKN65934.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN65934.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN65934.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN65934.1}.
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DR   EMBL; AJLS01000124; EKN65934.1; -; Genomic_DNA.
DR   RefSeq; WP_007086613.1; NZ_AJLS01000124.1.
DR   AlphaFoldDB; K6DCA8; -.
DR   STRING; 1117379.BABA_18097; -.
DR   PATRIC; fig|1117379.3.peg.3747; -.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000006316; 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:EKN65934.1};
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:UP000006316};
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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          173..225
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          233..448
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   457 AA;  52607 MW;  DBBCAFBA07F88968 CRC64;
     MIRSIYTKNI LNYFFVIIVS LILSFVITFF LFQNQVTQNR EAEVIEQGKA IIHLYQRLDK
     SGFNEYLNSL SSLPYDVYIY NQNGLASKSP QAAKKRELNR KNIDYVLDGG VYRNISGRHH
     MSVGLPFDIK NEPYALFITP SLKEQFSQIR SIILTALFLV LLLGISLILV TTKFLVRPLA
     HITNATRQLA RGNFQVRLHV KSKDEIGQLA KSFNFMVEEL EKTEQMRKDF VANVSHELQS
     PLTAIKGMVI ALKDGVVDHS EQKRYFGLME QESDRLSSLT KQLLNLSILE AGKSPFHPKR
     FRLDRQMRNQ LVALQPLWAE KQLDVDFDLP NIEIFADEGL LNQVWTNLYV NAIKYNWQNG
     KITVQGYDFE DEIEVVISNT GQGIPIEDLP YIFERFYRVE KAHTRAAESY GLGLAVAKRI
     IELHNGEISV TSTEGQETTF KIRIAQNSKR RVHDEKR
//
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