ID B8J427_DESDA Unreviewed; 1007 AA.
AC B8J427;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ddes_2176 {ECO:0000313|EMBL:ACL50072.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL50072.1};
RN [1] {ECO:0000313|EMBL:ACL50072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL50072.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001358; ACL50072.1; -; Genomic_DNA.
DR AlphaFoldDB; B8J427; -.
DR STRING; 525146.Ddes_2176; -.
DR KEGG; dds:Ddes_2176; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_314172_0_0_7; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; cd00088; HPT; 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; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; SM00304; HAMP; 1.
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; 1.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACL50072.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 231..283
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 326..550
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 635..755
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 822..924
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 542..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 687
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 861
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1007 AA; 108612 MW; 5DFE8FF96121E060 CRC64;
MSIRALIKTS NMAQLCLVLL LSLCTGWLGR SLYEINGLLH NYHHLESLLA EIGGISRENY
RAALDYISTG DTFHLERWRH LLRMERGEAP RPSTAQIAPG ERRSLTSLVD GLETTGPVRA
QVQSIVAQLV LLESMTEAAV RNALKSGPEA SVAQARQDRQ AALLWVHDNG LARIPDSIAE
AARRLGDKQR AEFLARLGER EAPLRWTLVA ALAGLALLGS SVLGNAYIFQ SRIANPLDRV
SRYAESVAAG LDPLPLHLRH RDELAVMFAS LQRMKGTLYS RIRELREAEQ RARRSRQQAV
LARSQALTSL ELAQRASHVQ DDFLRRISHE IRTPLNAIIG MSYLSLQTDL NGVQRDYLAQ
INKSGSVLLD MVNRILDFSS ASEGSIRTER KVFAVADLMD LLRQSVAGLA LEKRLRLNFV
LDPSIPAVVA GDERHLEEVL RILLDNAVKY TASGSVDFRI LPSGEPPMRK GAIRLLFVVS
DTGPGLGEEQ WKKLFEPFTL GDESMTRSFS GLGLGLALAR QLVSLMGGEL KVGSVPGQGS
RFSFSVDMEQ PDASGGCEDA EQPADGAAGN RSSIRSGPPD VSGVSGLPET PSLTGPAYPA
ALPHMPILPG PAGMAGPQAE APAGDSVGAP STAFAVLVVE DNEINAQIAR ELLEQAGLEV
LLAANGQEAL DLLDNPVHPP LGLVLMDVQM PVMDGLEATR RIRAMGISPV DLPVVAMTAH
TDMASRMDGK DVGMNDYLTK PVNPETLYAT LEKWLVGGLG RNPVKQAHED GGAAELPENG
SQGACTPAGR GMVAPATAAL PDAAQAVSII NVESGLATVG DNRKLYFELL QRFVDHYGDS
PARLRKMLES GNLKGAARMA HTVKGVAANL GVERICELTR TMEEFLPHNL PEHAVLEAFE
VEMGRVLDYV RSMGRHTCRT ASGSGQLAEE HRAALLAFLE DLPRRMETDW GAMESAMENF
SLLADGTPHA EGVAAILTAV KDFDMGGAGC LADNLRDSLL RESATKA
//
