ID A0A0F0KSR3_9MICO Unreviewed; 568 AA.
AC A0A0F0KSR3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=tcrY_2 {ECO:0000313|EMBL:KJL23524.1};
GN ORFNames=RL72_01944 {ECO:0000313|EMBL:KJL23524.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL23524.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL23524.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL23524.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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};
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:KJL23524.1}.
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DR EMBL; JYIT01000076; KJL23524.1; -; Genomic_DNA.
DR RefSeq; WP_045250634.1; NZ_JYIT01000076.1.
DR AlphaFoldDB; A0A0F0KSR3; -.
DR PATRIC; fig|582680.7.peg.1990; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000033448; 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; cd06225; HAMP; 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 InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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 PRINTS; PR00344; BCTRLSENSOR.
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; SSF158472; HAMP domain-like; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KJL23524.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000033448};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJL23524.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..254
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 269..546
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 549..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 60897 MW; 1A86EA7F2707B13F CRC64;
MGEPDAITRW WRRISLRAKV TGVTVGVLAL GLIVTGIGTM PILRNLLIGN VESQLPALVT
SDLATITPNA AGGFSAALKD ERPGLSEYFV AVYDAQGALV FSGGGEAKAT KPEFPTTYTL
ARATLDAGRT DPIVLRGADG SEFRAAVAVR EDPTSNITFI QFVALSLNEP DRIIATFFGV
FTTVALVTII VAALATRGLV TLTFRRLGRV ESTAMAIAAG DFSQRLADLE PTTEVGRLNG
AINTMLDRLD ASIAQRDRSV QQMRRFVGDA SHELRTPLVS VRGYAELYRM GAIKGDEDTA
RAMDRIEKEA LRMGVLVEDL LALARLDEQR ELTIEPLDLR PLAQDAALDL RAAAPERTVT
VVDMTAEAPQ AAAAEPSVSP ITRPAPTARA ANARGRIPAI LRRRPREDSP VPEIDFSEAV
VAPVSTPPIV LGEENKVRQV IANLLGNARR FSPGDSPIEV VVGADRHRGV GWFSIVDHGE
GVPEQIRDQI FQRFWRADSS RTRDTGGAGL GLAIVASIVR ALNGSVQVTE TVGGGATFTV
SLPLAPSRAT PEHLLQDTQP IEPLDLPR
//
