ID A8FRR8_SHESH Unreviewed; 567 AA.
AC A8FRR8;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Sensor protein {ECO:0000256|PIRNR:PIRNR003167};
DE EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003167};
DE Flags: Precursor;
GN OrderedLocusNames=Ssed_0930 {ECO:0000313|EMBL:ABV35541.1};
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35541.1, ECO:0000313|Proteomes:UP000002015};
RN [1] {ECO:0000313|EMBL:ABV35541.1, ECO:0000313|Proteomes:UP000002015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35541.1,
RC ECO:0000313|Proteomes:UP000002015};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|PIRNR:PIRNR003167};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000821; ABV35541.1; -; Genomic_DNA.
DR RefSeq; WP_012141277.1; NC_009831.1.
DR AlphaFoldDB; A8FRR8; -.
DR STRING; 425104.Ssed_0930; -.
DR KEGG; sse:Ssed_0930; -.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_000445_20_10_6; -.
DR OrthoDB; 9811306at2; -.
DR Proteomes; UP000002015; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR CDD; cd22899; NarQ_sensor; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.20.120.960; Histidine kinase NarX, sensor domain; 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; IPR029095; NarX-like_N.
DR InterPro; IPR042295; NarX-like_N_sf.
DR InterPro; IPR016380; Sig_transdc_His_kin_NarX/NarQ.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF66; NITRATE_NITRITE SENSOR PROTEIN NARQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF13675; PilJ; 1.
DR PIRSF; PIRSF003167; STHK_NarX/NarQ; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR003167};
KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR003167};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR003167};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR003167};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003167};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003167};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003167};
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 ECO:0000256|PIRNR:PIRNR003167}.
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..225
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 367..564
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 210..244
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 567 AA; 63599 MW; 34DC3EDFCFDA5577 CRC64;
MKKGSLTSTI LGLMLTLILL SSGLATFSII NLSYSLGDAK AINASGSLRM QSYRLMFYAN
SGSDEADEKI EEFENTLYSD ALKRSQAWYS SKESTDQYLL VIEKWKVMKY YIQQENSRLY
AAALKDFVDT IDLLVLEMEH HAAFKIKLLA ASQIFGLGLM LFIAFLAVRF TKKKVVTPLH
KLMESANTIS KGNFDIKMPP TDYVELSALS NALESTAKEL STLYKDLESQ VKEKTHALTR
ANDELTLLYD NLVMLHSGTL DIDTLKQALN QLRAHEPHSF LRLVICQDEE EKQVIEADGG
WPLAASNQLN FPLKFEDNEL GYLEVISTQQ PNHPLFENFA IMLARSIVIY SAGEQKQQLA
LMEERGVIAR ELHDSLGQLL SFLKIQVNLL SKGLDSACRS PQVEQQLSEI NEGVNTAYVQ
LRELLSTFRL TIKDPNLSHA IEAMLEQLRS QSDVNISLDY KLPLQLLGAH QHIHVLQLTR
EATLNAIKHA DAKHIHIRCF LSSPTDVTIS ISDDGVGIEQ LRERDQHFGI GIMHERASRL
SGIVEFSSNP EGGTTVTLTF PPQQEPS
//
