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Database: UniProt
Entry: A0A497XDY0_9PROT
LinkDB: A0A497XDY0_9PROT
Original site: A0A497XDY0_9PROT 
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
//
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