GenomeNet

Database: UniProt
Entry: C0FZI2_9FIRM
LinkDB: C0FZI2_9FIRM
Original site: C0FZI2_9FIRM 
ID   C0FZI2_9FIRM            Unreviewed;       304 AA.
AC   C0FZI2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Heme sensor protein HssS {ECO:0000256|ARBA:ARBA00040841};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   ORFNames=ROSEINA2194_04179 {ECO:0000313|EMBL:EEG91968.1};
OS   Roseburia inulinivorans DSM 16841.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=622312 {ECO:0000313|EMBL:EEG91968.1, ECO:0000313|Proteomes:UP000003561};
RN   [1] {ECO:0000313|EMBL:EEG91968.1, ECO:0000313|Proteomes:UP000003561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG91968.1,
RC   ECO:0000313|Proteomes:UP000003561};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG91968.1, ECO:0000313|Proteomes:UP000003561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG91968.1,
RC   ECO:0000313|Proteomes:UP000003561};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Roseburia inulinivorans (DSM 16841).";
RL   Submitted (MAR-2009) 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:EEG91968.1}.
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; ACFY01000167; EEG91968.1; -; Genomic_DNA.
DR   RefSeq; WP_007890372.1; NZ_ACFY01000167.1.
DR   AlphaFoldDB; C0FZI2; -.
DR   eggNOG; COG2205; Bacteria.
DR   Proteomes; UP000003561; 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.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEG91968.1};
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        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..80
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          88..300
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEG91968.1"
SQ   SEQUENCE   304 AA;  34454 MW;  EB43A3D2239464D5 CRC64;
     PGSIPVLGWL LIFNTLIAGL ITSFINAKLL EPITRLSKAM KEVSRGDFEQ HLETNSRIAE
     VGESYQSFNV MTKELRATEV LQMDFVSDVS HEFKTPINAI EGYTMLLQGE ELSPDQEEYV
     EKILFNTQRL SGLVGNILLL SKLENQNIPM KKTEYRLDEQ IRQAVLSLET KWTEKEIGFQ
     VELEEVKYTA NEGLFMHIWI NLLDNAIKFS PSKGTITMFL KQEQDSVKFI LEDEGPGIED
     DVKSRIFDKF YQVDGSHKAE GNGLGLALVK RIVDSAGGTI KAENREYGGC RFVIELPKQK
     DEII
//
DBGET integrated database retrieval system