ID A0A1G9M9F0_9GAMM Unreviewed; 779 AA.
AC A0A1G9M9F0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05661010_02349 {ECO:0000313|EMBL:SDL70315.1};
OS Halomonas muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=119000 {ECO:0000313|EMBL:SDL70315.1, ECO:0000313|Proteomes:UP000198654};
RN [1] {ECO:0000313|EMBL:SDL70315.1, ECO:0000313|Proteomes:UP000198654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14789 {ECO:0000313|EMBL:SDL70315.1,
RC ECO:0000313|Proteomes:UP000198654};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FNGI01000006; SDL70315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9M9F0; -.
DR STRING; 119000.SAMN05661010_02349; -.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000198654; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 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; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDL70315.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198654};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..111
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 158..379
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 530..647
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 676..769
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 507..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 579
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 715
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 779 AA; 85166 MW; 43C3AC66990EDAB9 CRC64;
MSLKFRLFPL LLGTPLMLLS IGAIYLLAQA QANHVLAWPV IALLLSVLVA LVVTYTAQRR
LFMALEAQRQ ALLRFASGDY GYRPDDRAPR ELVAFSNAMD ALGRHLQHAR ENTRQQIEWT
TRELQESMET IEVKNVELDM ARRRALQGNR SKSEFLANMS HEIRTPLNGI IGFCRLLGRS
HLDSRQREWL SHVETASNNL LTLINGILDV SKIEAGKLEL ESVTLDMVTL VDEVLVLLAP
TSQQKGLQLL GLVYDDVPAE LLGDPLRIKQ VLTNLVHNAI KFTERGDVIV RVFVIDTQDG
ETTLRVKVSD TGIGLSPEVQ KQLFQPFNQG SANRSRQYGG SGLGLTICKQ LVEQMGGEIS
VVSQAGQGAT FSFTLPLLGP TPPGERTAEL QLPEPGIALC ERHKPTRQAL SHLLDNWGAQ
VRIVDEKQLG EGFPSPPELL IVALDNDDLQ PSALARWGLH LASLSCPIVV LVNGNSYDLD
DSMLPGASEI LYKPVTRAQL ARTVRQQLEG NDEPAARKAA TQSHPGDRPR VLVVDDVASN
RLLIGELLAR QGIASVLAES GEQALALADD EAVDLVMMDI RMPGMSGVET LRRLRRLDGA
WAHCPIVALT AHALEDEARA LLDAGMQQVL TKPIDEHDLA RVLEDYLGLP SAEAIYRADD
LPVVDRLLGQ ATAGGSASLA NDVLALLLDG LDNSEAAIRQ ARAGGDPGAL LDAVHHLNGA
CRYCGVPQLT MLVDTLETRL RTQESGNIDA MLEAIFDAIQ RLRDWSDERD QSQQPPASS
//
