ID A0A2I0P349_9EURY Unreviewed; 689 AA.
AC A0A2I0P349;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CVV33_01620 {ECO:0000313|EMBL:PKL60640.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013820 {ECO:0000313|EMBL:PKL60640.1, ECO:0000313|Proteomes:UP000233538};
RN [1] {ECO:0000313|EMBL:PKL60640.1, ECO:0000313|Proteomes:UP000233538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-4 {ECO:0000313|EMBL:PKL60640.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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 -!- 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:PKL60640.1}.
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DR EMBL; PGYJ01000055; PKL60640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0P349; -.
DR Proteomes; UP000233538; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 2.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 175..225
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 226..297
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 300..352
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 353..397
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 584..682
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 689 AA; 78965 MW; E3DD186BCAADADDA CRC64;
MSTAWMVNIL TPKLSKLRFL WAKEPMSGAT LLALLLTFIV VPYWWLAVQW SDLVIPTPSV
QFAFATTTFL LALIVIDSLF IIRYYQIVRK NEFLKQARDL KISEENFRAL LEFAPFPIVF
SRISDSTIRF INQQTAEFFH TDVTVAIGKN VRDYYVQLDD RIPVLEQLRL NGRISNYEVQ
LLTSAGITFW VSLSANMIEY KGDLCLFIAF IDISQRKKLE EEIQKSEELY RSVVTASPDA
IAYSNLHGVM TMISPTGVEM FGGKTPNDFI GHHVLEFIHP DDAPQAQERM FKLISGEKIQ
LREYRGQRVD GTHFPYEIHS ELTHDDAGRP SGIVYVIRDI TKRKEADEVI RENEERFTTV
FQEVPVPLLI LDESGVILEI NAICEQRFQV SRDLVVGMLI TGLGVFTNNG EEDPYQFILG
HNPGKILETR LHLPDGTWRY VTVRTRTITL RRSPAILLLI HDIDDIRRAQ NALSQANTQL
NLLNSITRHD ILNRVTVVMS YSEFLHEKVD DPSSLTYISR IHESGKDIQH LIEFTKQYQD
LGLKKPEWQR IDRILKSRSV QPLLRDITVH LPVSSYEIYA DPMLEKVMYN LIENSCRHGL
TVTEFSIHYV EEDDHLWVRY TDNGVGIPLS EKKLIFKNGH GKNTGLGLFL IREILHITGI
TITENGIPGE GARFEMRVPA GSFRVVGSS
//
