ID A0A024K390_9MYCO Unreviewed; 858 AA.
AC A0A024K390;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN973_04931 {ECO:0000313|EMBL:CDO90535.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO90535.1};
RN [1] {ECO:0000313|EMBL:CDO90535.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO90535.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO90535.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO90535.1};
RA Xu Y.W., Yang Q.;
RL Submitted (APR-2014) 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; HG964446; CDO90535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024K390; -.
DR STRING; 47839.BN973_04931; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_1_11; -.
DR GO; GO:0005886; C:plasma 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 CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 387..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 634..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 858 AA; 92091 MW; CB4ED35A773EFFB9 CRC64;
MVDVSDVSLG DHHPKRGELR IYLGAAPGVG KTYAMLGEAH RRLERGTDLV AAVVETHGRA
KTAGMLEGIE IIPPRFIEYR GGSFPELDVP AVLARHPQVV LVDELAHTNT PGSKNHKRWQ
DVEELLDAGI AVISTVNIQH LESLNDVVAQ ITGIEQQETI PDSIVRAASQ VELIDITPEA
LRRRLSHGNV YTPERIDAAL SNYFRRGNLT ALRELALLWL ADQVDTALAK YRAENKITDM
WEARERVVVA VTGGPESETL VRRGSRIASK SSAELMVVHV IRGDGLAGLS ETRMNKIREL
ANSLDASVHT VVGDDVPTAL LDFAREMNAT QLVMGSSRRS RWARIFEEGI GTTVVQQSGK
IDVHIVTHEE SKRGFHIASF APRERRVASW LAAIIVPSLI CAVTVTVLDP YLDTGGESAL
FFVGVLLVGL LGGVAPAALS AVLSGLLLNY YLIAPRHSFT IAEPNSAVTE LVLLLIAVAV
AVLVDFAAKR TREARLAAQE AELLTLFAGS VLRGADLETL LERVRETYSQ RAVSMLREPS
EEDRAAGKKS YIVACVGKDP CVAVDSADTA IEVGDDEFWM LMAGRKLSAR DRRVLTAVAK
QAAGLIRQGE LAEEAGRTEA IVRADELRRS LLSAVSHDLR TPLAAAKVAA SSLRAEDVAF
SPEDTAELLA TIEESIDQLT ALVGNLLDSS RLAAGVVRPD LLPVYLEETV QRALVSIGKG
ATGFYRSAID RVKVDVGDAV AMADAGLLER VLANLIDNAL RYAPNCVVRV NAGRVGDRVL
INVIDEGPGI PHGTEDQIFE AFQRLGDHDN TTGVGLGMSV ARGFVEAMGG SIAAGDTPGG
GLTVVVELAA PPQPIGIQ
//
