ID A0A0H4C1F6_9ACTN Unreviewed; 450 AA.
AC A0A0H4C1F6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=QR97_01075 {ECO:0000313|EMBL:AKN68591.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN68591.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN68591.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN68591.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) 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; CP011799; AKN68591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4C1F6; -.
DR STRING; 1577075.QR97_01075; -.
DR PATRIC; fig|1577075.3.peg.227; -.
DR Proteomes; UP000036399; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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 NCBIfam; NF041732; hist_kin_CseC; 1.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR SMART; SM00304; HAMP; 1.
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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AKN68591.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000036399};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..224
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 232..434
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 201..228
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 450 AA; 48324 MW; 3306D88FF359141F CRC64;
MRGILRHPVR RMERAGLRTG LRWKVSAAIA LVAGLVAVVL SLVVHNAARV SMLDNARELA
NDRLLTAQRF YELGRGPVIP YVKIDDPSLP PALREKVERG RRVSDVSEHG GVADIWAAVP
AKDGHVLSLH SHLPDRRTDM LRDLDQALVI GSVAVVLGGS ALGVLIGGQL SRRLRKAAAA
ANQAAAGETD VRVQEAIGGV VRDETDELAR AVDAMADALR QRLEAERRVT ADIAHELRTP
VTGLLTAAEL LPPGRPTELV LDRAKAMRTL VEDVLEVARL DGASERAELQ DIMLGEFVAR
RVAAKDPDVT VRVVHESEVT TDPRRLERVL FNLLANAARH GRPPVEVTVE GRVIRVRDHG
PGFPEELLAE GPSRFRTGSK DRAGQGHGLG LTIAAGQARV MGARLTFRNV RPAGAPAGIP
AEGAVAVLWL PEHAPTNTGS YPMLPLSGGD
//
