ID A0A1Y5EEH4_9PROT Unreviewed; 888 AA.
AC A0A1Y5EEH4;
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=A9Q83_02645 {ECO:0000313|EMBL:OUR79866.1};
OS Alphaproteobacteria bacterium 46_93_T64.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1856292 {ECO:0000313|EMBL:OUR79866.1, ECO:0000313|Proteomes:UP000196525};
RN [1] {ECO:0000313|Proteomes:UP000196525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT within a complex community of hydrocarbon-degraders.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(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:OUR79866.1}.
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DR EMBL; MAAN01000009; OUR79866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5EEH4; -.
DR Proteomes; UP000196525; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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); 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..288
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 517..740
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 763..884
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 813
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 888 AA; 99202 MW; F9BA8D445EE635F1 CRC64;
MGLIKKTTTI ENPRLPIFKN LVLVLFCIVG VLAISAISYS VNDKNKEHLR GVFLQIAEDR
IWSLENNLSH DQDILRAIAS TMTTFNTVNQ TQFSELIGSL LSKDTSFKAV FWVQRGDNGT
NHDSEGSPKF PVVFGNPAGP FEKIQGLDMA ETVDIRDALF EARDSGQVAT SYASPLSKSN
SRGTEILIIL PIYESGVLLR RVRDRRQHLR GFIVGISEVA RIFRKSTARF TSQTNFSDVD
LFLFNKAAIL DKQLLFSSAE KHRSEYDLRG DIHLAYAIET VSRDWLVIIA PSSNFVTDPI
FIPAALIFAI GIIAVLALTI YVYQTLRQTA VIKLKVAEKT SDLKSSERRF RRLFENSEIS
IWREDYSNIY SALDKLRAEG VQDIRQYLIE NEQSVWEMAA SVKVTDVNAA TLELFGAKSE
DDFIFQIDKT FGSNTIEVFR DQLCAIWNKE KMFRAEAEFL TIDGQSIDCI LSLPLPETEE
GMRSVPVSIL DITDRKRLEK QVQHAQKMKA VGQLTGGIAH DFNNILGIIQ GNFEILLHSL
NGNENAKNRI EAGLKGTARG ANLTRKLLDF SRKDAGSIQR ISINHFIRDM EDLIAKSLTV
SISVDLRLDN DAWLVDIDPG DLQDVIINLA LNARDAMPDG GNLMIRSRNK VLDEIYTRLI
PESKAGEFVQ ISVSDTGHGM EAEVKEHVLE PFFTTKEQGK GTGLGLSMAY GFIQRSGGHI
EIKSEQGEGT TIHLYLPKAE KKLVSDQVTD TTETVSLPTG SGTILVVDDE EDLREIAVFH
LNDLGYQTLT AENGDKALEV LGDGHDIDIL FSDVVMPGDM DGYQLAVTAH EQYPNLRILL
TSGFTNKRAK LRGAEDKYLV NLNDRILDKP YNRAELAIAL KKTLNMQN
//