ID A0A1M7HIF4_9PROT Unreviewed; 781 AA.
AC A0A1M7HIF4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05216428_1213 {ECO:0000313|EMBL:SHM28093.1};
OS Nitrosospira sp. Nsp11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1855338 {ECO:0000313|EMBL:SHM28093.1, ECO:0000313|Proteomes:UP000184455};
RN [1] {ECO:0000313|Proteomes:UP000184455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nsp11 {ECO:0000313|Proteomes:UP000184455};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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; FRBV01000021; SHM28093.1; -; Genomic_DNA.
DR RefSeq; WP_072768884.1; NZ_FRBV01000021.1.
DR AlphaFoldDB; A0A1M7HIF4; -.
DR STRING; 1855338.SAMN05216428_1213; -.
DR Proteomes; UP000184455; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SHM28093.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SHM28093.1}.
FT DOMAIN 5..112
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 255..498
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 500..636
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 660..776
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 55
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 709
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 781 AA; 84711 MW; EC14ECD06B65CCC0 CRC64;
MTSKNDALLE RLLAMFRLEA DAHLQAMSSG LLALEEKPLD TRGADIIEAI LRGAHSLKGA
ARAVNFTQIE AVCRSLENVF SALKDKSLAI SSPLIDLLLQ TIDALSGLVA GDGSVSGTQK
SLLPKMMRQL DDILKRPLHE LASHTAAPQA APLLPLAASD ESTESGSNMA AQRAASAASH
ASATIRVPIA KLEAILRQVE ELLLPRLGVG QRAKELSEVT AALAAWKKQR LQIQSAMRIV
DRELTFNLKD NRTFRGKHEL PKLLKYLDAE PLHMKALESQ LARLQRAAEQ DHRTLAGMTD
YLLQDVKEMQ LLPFSTFLDI LPRFSRELAR EQGKSLELVI RGGEIEIDRH ILEEMRDPLI
HLVRNCIDHG IEQSAARLAK GKPSYGKITF SCSRSDSGTA EILVTDDGAG INVAMVKAAA
RKLGVISPEE MEQLGEFELM ALAFQSGVTT SPIVTDISGR GLGLAIVREK VEGLGGSIVV
RSNADIGTVF RILLPLTLAN TRGVLIHAGG QLFVIPSNSV ERVLLIANSE IQTMENRETI
LVDKQPLSLA WLSDVLELRP RVAEVEARTT PAVVLGSGLG RVVFLVEEIL GEQEILIKGL
VRPLTRVRNV TGVCVVGTGL LAPVLDVPDL LKSAVSRSAA VRVPTRRLSA EKHETSSEQS
ILVVEDSITA RTLLKHILES AGYRVTTAVD GVDGYTALKT GAFDLVVSDV EMPRMDGFAL
TAKIRADKQL PELPVVLVTA LDSQNHRERG IEAGANAYIV KSNFDQSNLL EVIRRLISLG
T
//
