ID A0A3S2Y3S6_9PROT Unreviewed; 1222 AA.
AC A0A3S2Y3S6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EOI86_00165 {ECO:0000313|EMBL:RVU37759.1};
OS Hwanghaeella grinnelliae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Hwanghaeella.
OX NCBI_TaxID=2500179 {ECO:0000313|EMBL:RVU37759.1, ECO:0000313|Proteomes:UP000287447};
RN [1] {ECO:0000313|Proteomes:UP000287447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gri0909 {ECO:0000313|Proteomes:UP000287447};
RA Kim J., Jeong S.E., Jeon C.O.;
RT "Gri0909 isolated from a small marine red alga.";
RL Submitted (JAN-2019) 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}.
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:RVU37759.1}.
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DR EMBL; SADE01000001; RVU37759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2Y3S6; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000287447; 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; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 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 Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000287447};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..182
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 299..369
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 373..425
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 564..785
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 806..930
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 963..1079
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1127..1221
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 933..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 862
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1012
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1166
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1222 AA; 133306 MW; 42C3B9743D12CE75 CRC64;
MVRFLSLLVS LSVAIGLVWA TYLYERSLAV DRTNLAAKTV SADLNRLAGS LEQILNHHLN
LTRALAAFVR TNPEITEDQF NAYADELVRG EVGIRSLQLA PDGVVTYVTN IEENARALGH
DLLADPNRRD LVLKSIQNKE FVIAGPIDLI QGGKAVIARQ PIFLKSTDKN DEFWGFATVL
IDPIVLFRES GIADGLPGLR LAIRGKDGLG AQGDTFYGDP KVFSSVAAEV PVHLAVGSWR
LAASWTPSKQ NELDEPAPFV WGAGLAIAVL AALFLFTLLT RPEQLRKEVQ QATEASKLSE
ERFADFANAA SDWLWEMGRD FRVTYVSDRA EEVVGVPAEV QVGRSLSELI GPDYFTEKWS
EARKTLKERR ALRNFVYTRR HKDGYLQYLS VSGVPIFDSD GEFSGYRGTG ADITDQVVAY
ERAQIAEQHL RTAIESLEDG FVLYDADDRL SLCNERYKEI YAESADLIVE GQTFEEIIRI
GAERGQYPEA IGREAEFVAE RLRAHKKSNT LIEQELPNGR WLRIAERRTP DGGIVGFRVD
ITQLKRAQEA AVAASEAKSQ FLANMSHEIR TPLNAIIGLS TLTLKTEMNA QQSEYVQTIH
SASKTLLGIV NDILDFSKIE AGRMELEEAD LDLEKILKDL SFIMVGRASG KPIELIIDAP
AMLPANLQGD AMRLGQILSN LATNAIKFTE EGEVVVSLEF SKRNETEMDI RFEIRDTGIG
ISENLHDGLF EPFAQADVST TRKYGGTGLG LPIAQQLVEL MGGEIGVYSG EEGGSTFWFT
AVVGLSKTSV VGDDTSSRAA ALKSMGVLLV IPNSALRESV RGMLGPLFGR IACVSNTKDA
LAALMRGAME TGGTPYDLVI FDCDVEQDGP LNAARKIQSA VTNDDPPNLF LLVRHGHELN
LSEVTDLGAV EVIAKPVIPP DLVRKIEAAF SGETRDADEP PLAGRGANDD EHVPPEVQIG
GMKVLLVEDN DINRRIATGL LERHGVDVDF AENGRIGVEK ALAGDYEAVL MDVQMPVMDG
IEAAGEIRKH PDMADLPIIA LTAHAMASAR DGCFEAGMND HVAKPIEPGV LFETLARWRT
TKNTTAIENV ASDAGDLAEM SKGISPSSLN DFTGIDMTGL KVITGGDEQT ALSLLRDFCE
EYAQESEKIR AAWEAGAVND AVERAHSLKG VSGNIRAVHV HDVVTKLEGA LKQNVADEKV
PMLLDDLFKA MSEINEMVAA QA
//
