ID F5LR32_9BACL Unreviewed; 455 AA.
AC F5LR32;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9413_2251 {ECO:0000313|EMBL:EGL15111.1};
OS Paenibacillus sp. HGF7.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL15111.1, ECO:0000313|Proteomes:UP000003445};
RN [1] {ECO:0000313|EMBL:EGL15111.1, ECO:0000313|Proteomes:UP000003445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL15111.1,
RC ECO:0000313|Proteomes:UP000003445};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (FEB-2011) 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}.
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:EGL15111.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFDH01000125; EGL15111.1; -; Genomic_DNA.
DR RefSeq; WP_009676456.1; NZ_AFDH01000125.1.
DR AlphaFoldDB; F5LR32; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000003445; 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; 1.10.8.500; HAMP domain in histidine kinase; 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:EGL15111.1};
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:UP000003445};
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 9..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..229
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 237..452
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 455 AA; 50739 MW; FFE67FAFA36F6F1A CRC64;
MIRSLYIRVV LTFLVSVIAG TVIAFFVSTW IFEDKLNLNA QINLRNFGQD IVRIYKTLPL
READSFVSDM KQLDSYHIRI YEATGGFQSY GKLNGHKPAA VTMEQLKKVM DGGVVQDTPN
GIASVLLGLP LKTEMGTKAM FLETLAPPSA TFVARWGIIF ATSSLIAGSL LILVASIFLV
RPIKKLTKAT KRIAAGDFNV KLNIKQSSEL GTLARSFEDM MHDLKQLEQM RREFVTNVSH
EVQSPLTSIS GYASALKQVG LSDHERSRYL DIIIAEAKRM SKMSDSLLKL SLLESQSRQL
RLTTRSLDEQ IRRVIVALQP QWNARRLQFE LDLDTIQVTA DHELLNQVWT NIIGNSIKFS
EDGGMINVSI GQDIKNVTVR ISDTGIGIPL DDQKRIFERF FKADRSHSRK VDGSGMGLAI
VKQIVSLHQG DIRVESELGQ GTTFIVALPI TTPTD
//
