ID A0A5K8AEE6_9BACT Unreviewed; 1230 AA.
AC A0A5K8AEE6;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DSCOOX_42430 {ECO:0000313|EMBL:BBO91063.1};
OS Desulfosarcina ovata subsp. ovata.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC Desulfobacterales; Desulfosarcinaceae; Desulfosarcina.
OX NCBI_TaxID=2752305 {ECO:0000313|EMBL:BBO91063.1, ECO:0000313|Proteomes:UP000422108};
RN [1] {ECO:0000313|EMBL:BBO91063.1, ECO:0000313|Proteomes:UP000422108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=oXyS1 {ECO:0000313|Proteomes:UP000422108};
RA Watanabe M., Kojima H., Fukui M.;
RT "Comparative genomics of hydrocarbon-degrading Desulfosarcina strains.";
RL Submitted (NOV-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 membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; AP021879; BBO91063.1; -; Genomic_DNA.
DR RefSeq; WP_155312038.1; NZ_AP021879.1.
DR AlphaFoldDB; A0A5K8AEE6; -.
DR Proteomes; UP000422108; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 2.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029150; dCache_3.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P_dom.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF14827; dCache_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; 2.
DR SMART; SM00091; PAS; 3.
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); 3.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000422108};
KW Transferase {ECO:0000256|ARBA:ARBA00022777};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 357..409
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 434..485
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 489..535
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 562..614
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 615..662
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 767..989
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1017..1135
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1066
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1230 AA; 137121 MW; 399BC04404C6C178 CRC64;
MPLRTRRLTE SPVFLFGVLG LVTIGLGLFF HHNRMTKQNG YLAHQQEIIG TTYRASVEMY
RLAMESFYKN IVCRPDITEI FAEGIEHVGS QRDWAKGRLY RALYSHYRAM KANNLLQLHF
HQADGTSYLR FHKPDRYGDN LFELRPSIRI VNTEQHPVYG FETGKVRSGF RYVYPIAWQG
RHIGSVEVSV TTKAIRDAMD SLSPNWEYGF LLNRERTLPL IFSEQQWLYR PATIHPDFLV
EDADALLPES PPPLSADATS INRRLRYNPQ VQDALSRGAP ITLGASTGYR YYTVCLMPMA
DVAGNVAGYL VTYSKDRVLA TFWEEFLIST IGVLAALGLI TALIMGLRRR TAALDLEQRN
LKIMTNVLAE GIFVIDQNGS IVRINSSACQ ILGYESDELI DQPIHERLHK HGGNQFVDQA
DCPLFKMVNS GQPYDGEEQF QHKDGSILIV EVASRPIWTK GGLVGSVTAF HDVTRRKRTE
AALRKSEETA RKLSIAVEQS PASVVITDLD GNIEYVNPKF VEKTGYTLEE AVGQNPRILK
AGTMDPSIYA GMWQTLTAGR VWAGELHNRR KNGEYFWESA SISPIRDKHG ETTHYLAVKE
DISGRKQMEA ELLEKELIQR TLMEHMPVGL VIVDAQTRLI EMVNPTTADL FGTSEETIVG
NQCHRFLCPA EVGQCPILDC GQTVDSSDRV LIQYDRTPLP VLKTVTRIMI NGREKLLECF
IDISSRIAAE EALKSVNKKL KSAIVQAEML AAEAEAANRS KSVFLANMSH EIRTPLNAIL
GYSQLLQQDA SLSREHLEQV RTINRSGDHL LELINGILEM SKIEAGHIQA QNARMNIDRL
LDDIHAIFQL TCRKKGLTLQ MERFGITPGT LIADQGKVRQ IIVNLLANAV KFTVRGGITL
RSTITPHGLE RWNVCIEVID TGSGISPAEQ PRLFQAFEQT ASGQRVAGGT GLGLSISRAY
ARSMGGDLIL VRSDTDQGAV FRLTFPAGRS QGHEDAADPP DMQQVVTGLQ PDQPPIRILI
VEDDPVSRQL IKKLIKDVGF DARAVANGEL ALEMIEGFLP DVVLLDVRLP GIDGYETVRR
IRRLSTGWRT RIIIVTASGV TADEVCRQAS AAGADDYVTK PFKIGEVLNK IKLLCNIAYA
YGRTPIDDPR ADAHSIESAP STLPEDLREA LRNAVEMGDM TAFESLVAQV ANVDSRLKDR
LSNLARRYEY MALLELLMPA LPVEAEPVAD
//