ID H8YYP2_9GAMM Unreviewed; 1502 AA.
AC H8YYP2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Thi970DRAFT_01240 {ECO:0000313|EMBL:EIC23568.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC23568.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC23568.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC23568.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH603168; EIC23568.1; -; Genomic_DNA.
DR STRING; 631362.Thi970DRAFT_01240; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_248614_0_0_6; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; cd06225; HAMP; 1.
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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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; SSF55781; GAF domain-like; 1.
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; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002964};
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 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 353..406
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 429..484
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 738..958
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 978..1100
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1126..1244
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1291..1395
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1399..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1032
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1177
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1330
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1502 AA; 162732 MW; 3FADF63125D15291 CRC64;
MKIHNALSNR LGWLRSVSSS TWKNSRPFAS LRFRLSFSIW LMLTVCTIAG GLLLGELFQR
QVVANKGALF FHIAESLVNQ LDRDMASRLD EIGIHAADQR LIDPSFSPEQ RRALLSRWRA
GSSFAWIGLL NREGRIEVAS DGRLEGSDVS AREYFKAAIG GEPYAGDVHE AWLLARHLPP
PRHDSLPLRF VDLAQPIYGA ADAPTDAPTG APIGVLVAHV GWDWAGDARD GLLGPLGDEH
GLEVVIFSSE GKALLGSEAL LKGTREPPLP SLTQGGDPRG DYRLMADKDG HSYLVGIGVS
HGFDDYPGLG WRVTVSQPTS IALAEGSTIK HRLWMIGALG AFALGWLVWA AVGRLVSPIR
ASVEAACRIS SGDLAVALPR VTGHCEAAEL CRALDAMVAT ILAQKAALAE ANEVLERRVT
ARTQQLAASE GRLQAILSSM SDGILQVDSE GRMTMANAAV EKMFGYPEEA LLERNLSLLI
AEPERLAEDS HLCWDFISRD DLSERLEVFG RHANGTTVPL EISRAELLDE SGRSCIFTLR
DIAERYRDER HLAEGHKTLE KIASGQTLAV VLNRIVELAE LFIPDSRCSI MLVDQPADTL
RMGAAPRLPA ALNALLDGIA CGERCGSCAT AAVSGEAVVA EDLARHPDWV ALRQVTAAAG
LRACWSVPAK DEDGDVLATI AIYINESRPP SDRELDRIGI PAHLLAIALT RHNRDKELIV
ARHKAEEATR AKSEFLANMS HEIRTPMNAV INLSRLALKT DLDAQQRDYI EKVLRSGENL
LGIINDILDF SRIESGKMAL DAVPFRLIDL ISDVADVITV KADERELEVL FDIPPLERLL
FGDALRLRQV LINLLNNAVK FTLQGEVVLG IDVVDCSSDK VRLDVFVCDS GIGISRKQRQ
RLFRPFEQAD SSITRGFGGT GLGLSISRHL LGLMGAELSL ESALGEGSTF SFTLDFPLCE
EHEADKETPE QRPQIDRRIL IVDDNQVACQ VLQHMLGRYG AKAAAASDGR QGIAALREAA
RAGCPYDLLL IDYQMPELDG IATFKQVLQD AEIMPKPMAV LVTAFSSEEV AIKARKLGFA
NLLEKPINPA RLFEVLLDGG AGGPRARVAF QSGRPLAELD GIRGQRVLLA EDQDINRQIA
TELLESIGLR VTTANDGREA LEHLTAEPDA FDLVLMDLQM PVMDGFEATR QIRADARWAE
LPIVAMTAHA MSAERQRCLA AGMNDHLAKP IDIDALHAAL VRWIAPAGAS MPIPASVADK
VAMGEAAAET PMPSALPGID LAAGLRRVVN NRELHGKLLR HFRDGHRRDA ETISRALAEG
RWADARLVAH SVKGVAANLG AERLGSAAAR LEARLAAGDG LGDDLGEDSG EDSGQDSDQH
LNEALAVFAG ALEEVIGGLD DFLPDDRPEP NRAEPEAEAP NLDAVAPLLS AIAREVESDL
GAANDHLALL HKLLRASQVR DQMARLGRAM SDYDSDAALA ILREIAAALG LEIKLGLEIK
ME
//
