ID A0A3N1KSA6_9PROT Unreviewed; 715 AA.
AC A0A3N1KSA6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EDC65_5023 {ECO:0000313|EMBL:ROP81168.1};
OS Stella humosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Stellaceae; Stella.
OX NCBI_TaxID=94 {ECO:0000313|EMBL:ROP81168.1, ECO:0000313|Proteomes:UP000278222};
RN [1] {ECO:0000313|EMBL:ROP81168.1, ECO:0000313|Proteomes:UP000278222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5900 {ECO:0000313|EMBL:ROP81168.1,
RC ECO:0000313|Proteomes:UP000278222};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) 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 -!- 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:ROP81168.1}.
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DR EMBL; RJKX01000018; ROP81168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1KSA6; -.
DR Proteomes; UP000278222; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ROP81168.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000278222};
KW Transferase {ECO:0000313|EMBL:ROP81168.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..568
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 588..705
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 637
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 715 AA; 77286 MW; 7C7DF53ABEE17896 CRC64;
MNRFGGAWKL PIGRVAIAAW IIAGLAFSSL AIVLQLRDRT ATLENYRDLR AYSANAAADA
MNRIFGTMDI VFSQAISEWA RSGRPIEQLF LSLADSERRI SRALLAIDNF SIIAANGRII
HSLNPGAVGS DVSDREYFRI HAETDRGMWI GEPHSSRIVP GQRRMPVTWR ISDAAGGFAG
VLWASLSPDV LSEVLYNYRD TDDSFVALLS VAGATLATDR VGRYVAIPET VVGPATVDSR
TTIVQDATID GTVGTWHLAG RRIGDSGLKV ILGSTEQQML QAWDTRTSTI IVLILLVVLF
QGAFALAILR LAADERQATR AAETAAGRAM QADLSKTEFL AVMSHEIRTP LTAIIGMSEL
LEGADLRPLE RRQVQAIRTG GRQMLSVVNN VLDFTRLGAG GIELETIDFS LPALLEEIRT
TMGTAAQERG LALMIASEND DLAVLRGDPN RIRQILLNLV GNAIKFTERG GISLTAERLA
EAARIGGTQR RFVRFIVEDT GIGIPADRFD RLFQPFSQAD TSMARRYGGS GLGLAICKRL
VDAMGGRISV DSIVDAGTRF RFDIPLENGS AAIQEPTTET RVQASSLKLL VAEDVEINRE
LVRAMLTARG HRVTLVGDGS AAVAAVRAER FDAVLMDVQM PVMDGVEATR RIRALPGPER
DIPIVALTAN VLTGAHQSYL AAGMSACVDK PIAWNVLEQT LIRLAGSPAA ADRPA
//
