ID G2KRY5_MICAA Unreviewed; 736 AA.
AC G2KRY5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=MICA_2188 {ECO:0000313|EMBL:AEP10493.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP10493.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP10493.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP10493.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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; CP002382; AEP10493.1; -; Genomic_DNA.
DR RefSeq; WP_014103716.1; NC_016026.1.
DR AlphaFoldDB; G2KRY5; -.
DR STRING; 856793.MICA_2188; -.
DR KEGG; mai:MICA_2188; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR eggNOG; COG5278; Bacteria.
DR HOGENOM; CLU_022478_0_0_5; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000009286; Chromosome.
DR GO; GO:0016020; C:membrane; 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 CDD; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR007891; CHASE3.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PF05227; CHASE3; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEP10493.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000009286};
KW Transferase {ECO:0000313|EMBL:AEP10493.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 378..597
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 615..723
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 663
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 736 AA; 82629 MW; D26F462A657B1CA8 CRC64;
MKVRYYAIIG FLILVLLVNV LGVLPYIQWS SFRNADARVT VDYIVIGELH HLMNTMQDME
TGQRGYILTR DPDFLGPFLH LYDMRVDELD FADDGRIVSA PFLDQSVAPA HIVDEIRHLE
QKLADDADSL ALVNDLRTLV DRKRMVTNDT LRLVRDRGFD DAVQNIKSGQ GKAAMDDIRA
VVSQLIAIRE ESARTMLHET DLRMASYSRF VIAGNIVLGV LLLLSFWGLA ASRERAIRDR
RRIERTDEQL RAFIRHAPAA IGALDRDLRF VIASDRWSSE FDSHWYRSAT GMELKDVLPY
LQTRDDWKQA VEKCLNGETV VVSEDKITQP GRPAVWARWE LHPWGNVKGG QSDGIIISVE
NITKRKDMER MKDEFVSTVS HELRTPLTSI RGSLGLVAGG VAGVLPQKAQ ELVDIAYKNS
DRLILLINDI LDMNKLEADQ LELNMAPHDM GMVLQEMVEA NQGYADKYGV QLGLGPAPGP
VSVLVDQHRF QQVLSNLVSN AIKFSPRGAT VEAGYVIDGS RVRLHVRDHG PGIPRQFQSR
IFEKFAQADS SDARAQGGTG LGLSIAKGLC ERMGGWMYFE TEEGQGTTFF IELPVYNAAE
TANDEDPLVD QLKKSVLHVE DDPDFYRVIR SGLEPQIVVR NARTLRDADI MIDRRDFDLI
ILDLRLPDGS GLSLLEHIKH KDKCPIVVIS AYDIPDDIKP LAAACLVKAR TPESEMIEII
KTLLGETDKT VTGWKK
//
