ID A0A3D9HJG5_9PROT Unreviewed; 1285 AA.
AC A0A3D9HJG5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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=DFP90_10633 {ECO:0000313|EMBL:RED49056.1};
OS Aestuariispira insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Kiloniellaceae; Aestuariispira.
OX NCBI_TaxID=1461337 {ECO:0000313|EMBL:RED49056.1, ECO:0000313|Proteomes:UP000256845};
RN [1] {ECO:0000313|EMBL:RED49056.1, ECO:0000313|Proteomes:UP000256845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8488 {ECO:0000313|EMBL:RED49056.1,
RC ECO:0000313|Proteomes:UP000256845};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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:RED49056.1}.
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DR EMBL; QRDW01000006; RED49056.1; -; Genomic_DNA.
DR OrthoDB; 7991996at2; -.
DR Proteomes; UP000256845; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12913; PDC1_MCP_like; 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; 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 Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 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};
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:UP000256845};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 419..472
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 477..519
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 636..857
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1019..1138
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1177..1276
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1071
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1216
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1285 AA; 143235 MW; C482DAB104DD33E2 CRC64;
MAEQLEDKVG KALPRPVQWY ESLQFRLSIG LLVILGILIL AFMTVNQTLL RSVLIENNFD
LVEQAGTGLV TELGQQVEAT EALTRSIASL VERLPFDEKL YKQVVPHLMK TGGNEEIIAG
GGVWPEPYQF DPSRERRSFF WARKFDNQLK YYDDYNAPEG LGYHREEWYV PAKYVGRDRC
FWSKSYMDPY SLEPMVTCSV PMHREEEMVG VATVDVKLAG LQQFFATRAE KLGGYAFAVD
RNNKFLSYPA LDMVKVVNVP GKQNQAREFV TVREFATRHP DFKPIAARLQ EFSDQLLSLA
QEHGGYDPGL SELIANESYQ INRHEAQMIS ATFADPLSPG NGAGDFKSSV RFSMSKDLIL
GEPVLVSMFI MPKVYWKIVV VTPQQPLIDR ASEVTGQILT VLIAIILVSM AGAFLWLRRA
LVRPLAAMTG EISASPLGGV SVRPLREKGF TEIDLLGSTI NRMRDQLSMS FEELRESENR
FRLIAESLPE GLVIARRSDG KVLYLNRRLR ELFAIPPEED EHKLRFLDFY DDPADRAQLL
LKLQTTNVVS DFVIPARRLD GTRFWMSVST CAISFMGEDA LVTGVIDVTK RKQAEDEVAL
YRSHLEQMVE ERTAELEGAK QVALQAAAAK QNFLANMSHE IRTPLNSIVG IGHLLLMKEH
LPAQNRYLLN LNKAGKILLK IINDILDITK MDVGKLKAEA VEFDLDDVLD DLSIHIRPML
AEKSIDAYLL RPANLDRKLV GDPLKLQQVL LNLITNAIKF THQGYVECDI RFDPLDGDRA
ELFFNVRDTG IGIPKDKMES IFNAFTQADS ATTREYGGTG LGLAISKTLV QLMGGSISVE
SKPGEGSCFR FQVPMGLAAQ DKENPFAGLD SPVHVLTISN DERELNSLER LFSRLSMMPV
TAGFDAGAVD ILKAAAVSDH PFEVLLMDWD QDKPAKQAML AGLKASGVRD KLAVIAVTQS
ITTEDERMLD TGILDAVLSR PVRISRLKSS IGTLLNMEID APHLPLSPGG RDRPLADVRI
LLVEDNEQNQ FVVEELMGDA GAEITIAGNG RHALDLIRDR GADAFDIVLM DLHMPVMDGF
EAVRLIRRDF GPEELPVIAL TAEVFQEVVD KCHHHGMNDY LAKPINPSHA IEVISRWSRR
SGRDAVPMAK SEDLVAVPGD PLEHLSLEGG LANLDGRRSL YQKMLRDYLD KYSDFEGELS
ILLASGPSEE AARFVHTFCG LSGTIGATGL EKAARLFKKE LDDCRKNEDV VPPDPESLVS
ALGLLLLEIR RVLEEGFLDR DPTIH
//
