ID A0A1A1ZBW1_9MYCO Unreviewed; 729 AA.
AC A0A1A1ZBW1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A5724_05600 {ECO:0000313|EMBL:OBF41048.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF41048.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:OBF41048.1}.
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DR EMBL; LZHZ01000004; OBF41048.1; -; Genomic_DNA.
DR RefSeq; WP_067795248.1; NZ_LZHZ01000004.1.
DR AlphaFoldDB; A0A1A1ZBW1; -.
DR STRING; 1834117.A5724_05600; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000092025; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
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; SSF55781; GAF domain-like; 2.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OBF41048.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 384..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 614..727
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
SQ SEQUENCE 729 AA; 79991 MW; 17226E96D1D0DD8A CRC64;
MAERSERTTR VSRASTELNQ ALRDAREQSA ASRQILAALG RADADPGAIL DTILERAEIL
CRAQAANLYI PEGDAFRLSR ASGKIPEQFR RYLEDHPLAR NKSSTVGRAA VEKRTVQIAD
VLSDASYGRP DLQQLAGYRA LLSTPMMLQN EVVGVLSMWR TSAQPFNARE CELLEEFAVQ
GAIVMRQVAL LRELGSKVAQ LEALRDVGDA VGSTLDLDEV LDQIVSNAVR LTATDGGSIM
EYDEPSNSFH VRAAAGTDPD LLKALRAMVI DRDSTLVGRA ATAHRTLEVP DLTTVDLDPH
LEALYRNGWR SVLAVPILRG ERILGVLVIR RRSTGSFGPY VELLETFAGQ SALAIVNARL
FGELQTKTIE LEVASRHKSE FLASMSHELR TPLNAVIGFS EVLLDRMFGE LNERQDEYLR
DIWNSGKHLL ELLNEILDLS KVEAGQMVLE PATFNVTTAL EYCLAMVRER AAQHGITVDV
DVADEISTID ADERKFKQVA LNLLTNAVKF TPDGGSVSLR AYREQDDLEI TVTDTGIGVP
FEDQERIFES FQQGPRGAPK EEGTGLGLTL SRRFVWLWGG RMWLHSTPGE GATFGFSIPG
VLRRGAPAPD HLAAILLVDD DWASLDLNAA YLDGSPTRVL RAKDGVEALA IARTQLPAAV
VLEIGLPRRE GWQVLTELKE DPATADIPVV VATHVDDRTR ALSSGADVYL RKPIGREELM
DALKQVGAL
//
