ID A0A1G3MIV0_9SPIR Unreviewed; 595 AA.
AC A0A1G3MIV0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2004_11990 {ECO:0000313|EMBL:OHD29941.1};
OS Spirochaetes bacterium GWC1_61_12.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802180 {ECO:0000313|EMBL:OHD29941.1, ECO:0000313|Proteomes:UP000178922};
RN [1] {ECO:0000313|EMBL:OHD29941.1, ECO:0000313|Proteomes:UP000178922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHD29941.1}.
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DR EMBL; MIAU01000090; OHD29941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3MIV0; -.
DR Proteomes; UP000178922; 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; cd00082; HisKA; 1.
DR CDD; cd13704; PBP2_HisK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..595
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009597253"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..592
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 595 AA; 65565 MW; 0B11743BB5649E01 CRC64;
MKQRTIFCLV IFCLLASQAS AQYQLSEAEK RWLAEREEVV FAGQISYPPF EFIHPRYGDY
TGMSIDLIRW IATEYGFTTV FRPMPFAAAQ QAVVIGTADA MTGIFESEER RQRYDFSDEV
FAVPASIFVH AERNDIIELL DLDGKRVAVQ RGDYAIEYLG AQNIEVDWVY TTDFQTALAM
VAAREADALI GDEQIVYWHL YSASLTNTIK KVATALYIGS DCMAVAKGNS ILLSILQKGL
RKAKATGVLR TIGQKWLGVS FAVEEPGLDR WRWPLIIGLA LMAPLSLGVL LWTMQLRRLV
RSKTTELQNL NAHLRQSNES LSYANSQLMK DMEERARLAE EGRRLEARMI KAQSHESLAL
MAGNIAHDFN NSLMGIIAAI DSALALQPGE PLDETTRQNL ASAGGKAKSA GELARRMLEF
AGQSSFNRVN ITLNELLRDV QPLLAASTAA AIEIINAIPD EAIAIKGDPG QIKQAILNLL
INAVEASAES RLPVQLTLWR GQLAEPGRHQ ARAGNELPPD EYAHIRIQDT GSGIDRTIME
RLFDPYYTTK RAGRGLGLAA AAGIIKAHGG AITVESDRHH GSCFTIILPL VEPAG
//
