ID A0A1T1B7W5_9DEIO Unreviewed; 679 AA.
AC A0A1T1B7W5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BXU09_16920 {ECO:0000313|EMBL:OOV12472.1};
OS Deinococcus sp. LM3.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1938608 {ECO:0000313|EMBL:OOV12472.1, ECO:0000313|Proteomes:UP000191141};
RN [1] {ECO:0000313|EMBL:OOV12472.1, ECO:0000313|Proteomes:UP000191141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM3 {ECO:0000313|EMBL:OOV12472.1,
RC ECO:0000313|Proteomes:UP000191141};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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:OOV12472.1}.
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DR EMBL; MUFV01000003; OOV12472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1B7W5; -.
DR STRING; 1938608.BXU09_16920; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000191141; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 252..407
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 409..540
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 562..678
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 611
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 679 AA; 70608 MW; 6EDBFCDEB05DDE90 CRC64;
MNHRDATPPP GPAAGPAFRA DRDLSGALRG EWLALRADLC AGGDAAARAL HSLRAAAAVE
DDPALAAATD RAEQLLGSAQ VPVGGWEARL RELGLLESAR PEPAPPPPTT LPPVTPPAAT
LPSSTPAAPD PAASGSPDDD AQFVRMDVRK LDALLALAGE LTGARLQLQE RLAQARASQD
AGAWRSVQAS QHALKTLTDD LAREVLAARL QPARPFLLGF ERALRDAARQ AGKRARLVVG
ASGVELDRHT MDRLRAPLLH LIRNAADHGL EDPATRAAAG KSPVGTVRLD AYNAGGQVEV
TVTDDGSGVN FAAVRDSAAR RGVTLPDGAP LDAALPDSGP DGGLDEAALT ELLFTPGFSS
REQVTDLSGR GVGLDVVRTQ ARQLGGDVTL RSTGQGTTVT LRVPLTLATT RVAVVRCGEQ
LLAVPVTWVE RAGRAGPLRT LEGRRVLRVG DQTVPAAPLL ALLDGEAGAA GEPGTFLLVR
QGPQRLALLV DALMGEQEIV IKPLRWPLQG APHLEGAAIL PSGQVVPVLN VLALHLPAGR
PPAGRPPAGS LDGTPVPAAP PRVLLAEDTA VTRQLITQIL QQGGFEVLPV PDGAQALAAL
HAQPPDLLLT DVEMPELGGL ELVRRVRADP RTANLPVVLL TSLDSPGDRA AGAEAGADAY
LVKGEFSQEA LLHTVRRLL
//
