ID D5CS91_SIDLE Unreviewed; 902 AA.
AC D5CS91;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Slit_1594 {ECO:0000313|EMBL:ADE11827.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE11827.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE11827.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE11827.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) 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};
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DR EMBL; CP001965; ADE11827.1; -; Genomic_DNA.
DR AlphaFoldDB; D5CS91; -.
DR STRING; 580332.Slit_1594; -.
DR KEGG; slt:Slit_1594; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG4585; Bacteria.
DR HOGENOM; CLU_321287_0_0_4; -.
DR Proteomes; UP000001625; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 1.20.5.1930; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADE11827.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001625};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADE11827.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..346
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 441..493
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 708..898
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 673..700
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 902 AA; 100710 MW; DF04D965838B26C9 CRC64;
MKSPYTIRAQ LMALVAAVAL PMVGILAYTI YDNAKQQIVE AQTIARTLVV ASASDVDHVL
ITNRDLLRQI AKRSLIRKMD GKHCDQVLSD LHDLFPKSAN MTLIDIQGTA ICSVVPQTKG
KQVSVANAAW FKKSLATDGL VVSEPFVGPI TGRWVTVLTY PIHDDAGNKI GFLGLPLDLA
LYEPDLSDAQ LVPGTSIGVI TAGGAVVWRN IDADKWIGKD LSNNKEFEKI LAVKQGAIEG
KGFDSIPRFY YVSPIAWADW YVYVGIPTSP FYSQLRKMLV RNILFSLAML SFVFGVAWLI
ARRISNPISQ LTAVTRAISQ GSRVARAELV GPPEIREVAQ EFNEMLKIRW HTEAALRESE
INLSEALKIA RMGHWEYELI TDEFVLNDQY YSLHHTSAEK MGGYRMRSAE FSQRLVHPGD
AHLIDEYIQR SLSVKAPELH LQAEARIICG DGKTRWVLVR FKIEQDNNGV TTRLLGVNQD
ITERKHAEQT RQKLNRALVL VSECNALVIH ADNEQSLLSD ICRLTVESGG FLMAWIGFAE
HDANKTVRPV AQTGYEEGYL ESVNVTWADT ERGQGPTGKA IRTMQTVVNQ DCQFNSDMAP
WREAAIKRGY QSSIGIPLVI NGKAIGALTI NSADPFTFSK GEVVLLEDLA DNLSYGIQTL
RTRNEHQSAL TFLQKSELSL EQSNQQLRDL TIRREEARED ERKRIARDLH DELGQILTVL
RMDLSVMRMQ FGASNPALLD QIKNILSRVD STIQVVRDVA SKLRPGALEA GIVAALEWQV
AEFAKRSDIH FDLKIDESNI DLDDERATAI FRIVQESLTN VTRHAAAANV CVSLSRLQDN
YILEIIDDGR GFDTEMLSGR TFGLMGVRER SMMLEGTVDI RSSPGKGTHV TVYIPVMKRQ
KR
//
