ID A0A497XDY0_9PROT Unreviewed; 865 AA.
AC A0A497XDY0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DFR35_1869 {ECO:0000313|EMBL:RLJ65212.1};
OS Sulfurisoma sediminicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfurisoma.
OX NCBI_TaxID=1381557 {ECO:0000313|EMBL:RLJ65212.1, ECO:0000313|Proteomes:UP000268908};
RN [1] {ECO:0000313|EMBL:RLJ65212.1, ECO:0000313|Proteomes:UP000268908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26916 {ECO:0000313|EMBL:RLJ65212.1,
RC ECO:0000313|Proteomes:UP000268908};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:RLJ65212.1}.
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DR EMBL; RCCI01000005; RLJ65212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A497XDY0; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000268908; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; 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; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
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; 2.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000268908};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..372
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 397..451
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 469..692
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 719..840
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 770
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 865 AA; 93489 MW; 0970D167225E83CF CRC64;
MAMFTALISN AALLLAMVLI LDLARDDADG TARRLPAPLA GAILGVIAIG AMLAAYRAGP
GLIFDTRSVL FGASGLFFGP VPTLIATVIA AAYRLSLGGP GAIVGVASII VSGAIGILWS
KLRRGPLANI GWRELLALGL TIHVVLLGMF AVMLPSSTMT VAGVALPFLT LYPLATVAIG
MLIANRLGHE RTRAALTASE HRYRALFDSS ITPLVVMNPA DGRFIDCNPA AITAYRLPDR
DAVLGLTPLD VSAPQQPDGE DSATAATRHI ADCVRNGLAI FDWRHRRPDG EIWDAEVRLM
KFRQEERDLV QFSLTDITEL RRGEEARRTL MQAIEQAPAS IVITDMDANI EYVNPAFSRV
TGYDLDEVRG KNPRILQSGQ TPPERHVELW NTITSGQTWS GVLHNKRKDG SFYWEQAYIG
PVCDERGRIS HFVAVKENIT ERMLAEEELV RARDAAEGAT RAKSAFLATM SHEIRTPLTG
VLGMAQLLLQ DEVSESERRD YARTILNCGN SLLTLLNDIL DLSKVESGRI ELAAAPYAPG
QLLEEVADLF GQAAENKGVA LVVDAVDAGD TDRRYVGDPT RLRQMLSNYV SNAIKFSSAG
AVHLAVRRIA HPDGDVLRFS VRDEGIGIPP EQQELLFRPF VQLDSSSARA YGGSGLGLSI
VRSVAEVMDG SAGCDSVPGA GSTFWFEVPA QTLAAGVEAR AAPRGPADAG LAAGWRPRRI
LLAEDNAVNR KVVELMLRKQ GIEVISAEDG AAALAKLQSD AAPPDLVLMD CQMPVLDGFE
TTRRIRAWQA AEGRAYLPII ALTANAFEED RQRCLDAGMD DFITKPLNLP RLLAAFDSLH
RTAPGAAQAA RPLYDRRPDR GEPEK
//