ID A0A0S8E582_9BACT Unreviewed; 651 AA.
AC A0A0S8E582;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMJ65_07520 {ECO:0000313|EMBL:KPK42508.1};
OS Phycisphaerae bacterium SG8_4.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK42508.1, ECO:0000313|Proteomes:UP000051853};
RN [1] {ECO:0000313|EMBL:KPK42508.1, ECO:0000313|Proteomes:UP000051853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_4 {ECO:0000313|EMBL:KPK42508.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK42508.1}.
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DR EMBL; LJTR01000111; KPK42508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8E582; -.
DR PATRIC; fig|1703409.3.peg.3950; -.
DR Proteomes; UP000051853; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 432..651
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 156..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 73500 MW; E7818EFB5B10E2B0 CRC64;
MYRRLIILSI IILAALCGLL WMGYHSIRIR AQGLEGARLG EFAAVAEQIR QDVTRTLDEF
MQTEQNRPYT DYQYYYVPEN LAPGQQQMPV LRSPLAGRLE QGLAYGNFQI EPDGSVITPN
DNVDQRQDLT ESDNKLFAEA SSNKKNIQDN LLPALRGTTN GSLKMSSYSG SSIEPPKEPE
TLQPDRFAEQ AGQKAKLSQS YPIESLQSRG QKTQVIEQRR AVLEQNVISN RPAQLQAQIQ
ELSAQAEEMT GLDQRQTASP DESQTETVQV RVEPFFPVVV PGQPAGSDSA RQQAESIFGG
QVFLLRHVQI EDRHFLQGFR LNEKMLSEQI EQSASRFMRE GMAFELSPRK DARDDAEIAY
TAILNFGFGD LVLNLREIDP GWIDREIRHL RIWYFSIIAI VLLAVTLGLA SLWRSATAQI
RLAQKKDDFI SAVSHELRTP LTSIRMYAEM LEKNWVKSQD KAAEYYGNMR QESERLSRLI
ENVLDFSRIQ RGRKKYAFNA GDINKCVEDV VEMMRPYAAQ KGFSIRTEPG QIEQATFDSD
AVTQIVVNLL DNAIKYAREA ADKTITVRTR TDGKFTVIEV EDHGPGVPHR QRNKIFEQFY
RPTAEATRET AGTGLGLALV KRFAEAHNGF VEIISAKPTG AIFRVALATR I
//
