ID A0A1Y1RG64_9BACT Unreviewed; 805 AA.
AC A0A1Y1RG64;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B6244_10100 {ECO:0000313|EMBL:OQY27603.1};
OS Candidatus Cloacimonetes bacterium 4572_55.
OC Bacteria; Candidatus Cloacimonadota.
OX NCBI_TaxID=1971726 {ECO:0000313|EMBL:OQY27603.1, ECO:0000313|Proteomes:UP000192623};
RN [1] {ECO:0000313|Proteomes:UP000192623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) 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 -!- 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:OQY27603.1}.
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DR EMBL; NBMB01000037; OQY27603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RG64; -.
DR STRING; 1971726.B6244_10100; -.
DR Proteomes; UP000192623; Unassembled WGS sequence.
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; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 2.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}.
FT DOMAIN 2..118
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 140..186
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 210..262
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 439..658
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 684..800
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 733
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 805 AA; 91542 MW; 3F46C4D97CFB237E CRC64;
MKILIIEDDF IFLKLISKII ENNGHEPIAY TNAEDALERY QAEFFPLIVT DVGLPGIDGL
ELCRRVRAQP QGQYTAILVV TGTLKPEDLE IILDAGADDY IGKPFHTKML KIRLKISVQR
ARNQILKKEA DEALKSKESE LLLLKKSVET MQLGIAISDV DRKIIYVNQA IADMHGYRTE
ELLGQNVQNF APRELWGDVT QDQMRTFGRW NRESVNLRKD GHEFPVQLIS TVIKDEKDEI
VGVVTACEDI TERKKKEDQL RASRERFKNI FQSTTVSLWD TDFSRVMQRV RALPVSGADD
LKEYLDKNPD AVIRLAKEIK IWDVNQVTLQ FYEADSKDQL LGSFKKIFSS HSCCIFKKVL
VEMASGSDIF ETEIEGKTLK GRRMTLLMSV RIPKKSKDFS HILVSETDIT YLKQTERELV
RAKDMAESAN QAKSAFLSSM SHEIRTPLNS VLGFSQILHN KTRNKVYREY LKSIEISGKT
LLKLLNDILD LAGIESGKLK SKPVLSNLRL VMEEVKHAFL LKLMQKDVDF ILDLPDDLPK
EVHIDERRLR QVLLNLVGNA VKFTEKGHVK LSVRVVPHKL HKHIIDLIIS VEDTGIGIEP
EIQESIFDAF QQYRQKYEGA GLGLTIVKQW VELMNGSVRV ESQPDIGSVF ELELKGVKAP
GRVLDSYGTS SGLDYRRIVF NTSTILIADD VKSNRMLIKA ILKCSRAKIF ESQGGEDAVE
LAERIEPTLI LMDLQMSKMD SYNTVERIRT NPELEDVPII ALIVNASEKN RKHAISSGFN
GCIKKPIQIR ELFVNLMGHL DVSFY
//
