ID I4C4P0_DESTA Unreviewed; 1356 AA.
AC I4C4P0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Desti_1823 {ECO:0000313|EMBL:AFM24531.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM24531.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) 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};
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DR EMBL; CP003360; AFM24531.1; -; Genomic_DNA.
DR RefSeq; WP_014809677.1; NC_018025.1.
DR STRING; 706587.Desti_1823; -.
DR KEGG; dti:Desti_1823; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG3290; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_257289_0_0_7; -.
DR Proteomes; UP000006055; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 5.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; 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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..412
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 415..467
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 468..514
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 548..601
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 602..672
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 675..727
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 728..798
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 802..854
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 851..897
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 922..976
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 989..1212
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1232..1348
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1283
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1356 AA; 150994 MW; D35A5A539EC7AAB8 CRC64;
MSDTSPKQVA TPGKKARALS LLSFQTRLIW FCVLPLVVLA MFLAVTYVYT LQTQRNEDAE
HQARNVAMAI DQKIGSQMAA MQVLSSSPLL DDLQRFNEFY IVAQAFHRRF GSHIVLADTS
MQMLLNTRLP LGTPLPRLPL PKGRAAAPVA LETGNPAVGD VFFGPIAKEP LVAIAVPVIR
NGATKLLLIS VIQTSQFQER LEKVSLPSEW SLRLLDGTEE VMAHRSSPDT DNSSYSDSKR
FVAKSSLTPW SVVLEIPADV YRAPLFLATF VLAAAILAVT LISISGGWRA SRKLAASVRA
LVETRLRDVS ELSIMEIEAV RRILAHTAEA RELAESTLLE SERRYRDLYE NAPDMYVSVD
ATTSRVVGCN QTLSRMTGYS KEAIIGRPVL EIYHPDSRED ACKAFQVFLA AGNVHNIELQ
LLRADGSTIN VILNASAVCD ENGAILISRS SLRDITDLKR AEEIILESEK NHRLLIENLD
AGVVVHAPDT RILLCNRVAS EMLGVSSEKM IGKTSSDEDW MYVREDGSPL PPDEYPVNRV
ISTLEPISNC VVGMDRPGSN DRAWGLVNAY PAINEKNELE QVVVTFVDIT DRKRAEDALI
QSENRFRLLY EEAPVAYQSL DEDGYLLQVN MTWLQLLGYT RSEVIGKRFS DFLNACSRDH
FEEMFPEFKR AGHISGVEYR MVCRDESIID VSVDGRIVWT EDGKFRHSHC VFQDITQRKK
AERALLESEQ KYRATFNTAS VGIDLVAPQG TFLEVNSTLS EFLGYAPEEL QCLTVFDVTH
PEDIVRSKML HEAMIQGKTE GYRLEKRFLR KDGSTLWADV SVSALRDVDG TYRATVGVIS
DITQRKILEE ARSRLAAAVE QAAETVEITD AQGTIVYVNP SFERTTGYSL QEVVGNNPRI
LKSGRHDNEF YRHMWDTITH GKTWTGHLIN RRKEGTLFEE DVSISPVKAD SGEITNYVAV
KRDVTKEVSL QRQLLQAQKM EAIGTLAGGM AHDFNNILQV VLGFSELMLA AKSKEDSDYS
DLHKIHHAAS SGADLVRNLL TLGRKVETKP IPMDLNNQVR TVKKLLQRTI PKMIGIKLDL
AGDLMRMDAD PGQIEQIIMN LAVNARDAMG EKGTLTLKTE NIVLDEEYCR TYANTQPGQY
VLLSVSDTGH GMGRETLQRI FEPFYTTKEL GRGTGLGLSM VYGIVNQHGG HIRCESEIGL
GSTFRVYFPA IKAIEESPSG ETDKVLALGT ETILLVDDEE FVRDLGARIL RKGGYTVLTA
KNGLEALDVF KKESSRISLV ILDLIMPEMG GKGCLKELLK IDDKTGILVA SGSSADSTIK
ECFELGARGF VAKPFRLREL LREVRKILDR SYTDLH
//
